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COMMENTARY |
CRC Institute for Cancer Studies, The University of Birmingham, Edgbaston, Birmingham, B15 2TA, UK
Author for correspondence (e-mail: f.berditchevski{at}bham.ac.uk)
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SUMMARY |
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 Top SUMMARY IntroductionThe structural basis for...The role of tetraspanins...Signal transduction by integrin...The role of tetraspanins...Integrin-tetraspanin complexes...PerspectivesREFERENCES |
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Key words: Tetraspanin, Integrin, Migration, Signalling
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Introduction |
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TopSUMMARYIntroductionThe structural basis for...The role of tetraspanins...Signal transduction by integrin...The role of tetraspanins...Integrin-tetraspanin complexes...PerspectivesREFERENCES |
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. The LECLs of >50% of tetraspanins include a Pro-x-x-Cys-Cys sequence (the PxxCC motif), in which ‘x’ is any amino acid. In addition, various other residues (mainly in the TM domains) are relatively well conserved among tetraspanins (Fig. 1). A combination of all the above features distinguishes tetraspanins from a diverse group of proteins that have four transmembrane domains, some of which [e.g. L6 antigen (Marken et al., 1992; Wright and Tomlinson, 1994), il-TSP (Wice and Gordon, 1995) and sarcospan (Crosbie et al., 1997)] were originally described as members of the tetraspanin superfamily. Tetraspanins are implicated in a variety of normal and pathological processes, such as tissue differentiation (Boismenu et al., 1996), egg-sperm fusion (Le Naour et al., 2000; Miyado et al., 2000), tumor-cell metastasis (Boucheix et al., 2001) and virus-induced syncytium formation (Fukudome et al., 1992). Nevertheless, the biochemical function of the tetraspanin proteins remains undefined. No membrane or soluble protein has yet been shown to be a physiological receptor/ligand for tetraspanins [except for the hepatitis C virus envelope glycoprotein E2 (Flint et al., 1999)]. The N- and C-termini of tetraspanins, although well preserved across vertebrate species, exhibit no similarities between the individual family members. Thus, despite their relatively short lengths, these regions might have distinct functions. Computer-assisted analysis of the cytoplasmic domains of tetraspanins does not reveal any homology to well defined structural modules or motifs [except for the tyrosine-based sorting motif (see below)]. Given no obvious clues to their biochemical function, tetraspanins are predicted to represent transmembrane scaffolds that control the presentation and spatial organisation of various membrane complexes (Maecker et al., 1997).
Here, I discuss recent work concerning the structural and functional aspects of the complexes of tetraspanins with integrins.
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The structural basis for integrin-tetraspanin complex assembly |
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TopSUMMARYIntroductionThe structural basis for...The role of tetraspanins...Signal transduction by integrin...The role of tetraspanins...Integrin-tetraspanin complexes...PerspectivesREFERENCES |
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ß heterodimers that function as key adhesion receptors for the extracellular matrix (ECM). Since the first report describing the association of tetraspanin CD9 with IIbß3 integrin in stimulated platelets (Slupsky et al., 1989), various other integrin-tetraspanin protein complexes have been identified in many different cell types (Table 1). Although the association of certain integrins (e.g. 3ß1, 4ß1 and 6ß1) with tetraspanins is observed in all cells in which the proteins are co-expressed, the others (e.g. 2ß1, 5ß1 and 6ß4) form complexes with tetraspanins only in particular cell types*.
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Although the association of most tetraspanins with integrins can be observed only in the presence of so-called ‘mild’ detergents, the CD151-3ß1, CD151-6ß1 and CD81-4ß1 complexes seem to be more stable given that they can withstand conditions (e.g. the presence of Triton X-100 and Digitonin) that disrupt all other integrin-tetraspanin and tetraspanin-tetraspanin interactions (Berditchevski et al., 1997a; Serru et al., 1999; Yauch et al., 1998). This suggests that the associations of CD151 and CD81 with their respective integrins are direct. Furthermore, by directly interacting with the integrins, these tetraspanins might bring other family members into integrin proximity. A recent report suggests that the tetraspanin Tspan-3 functions in a similar fashion, although a specific ß1-integrin partner has not been identified (Tiwari-Woodruff et al., 2001).
The relative stability of the CD151-3ß1 complex has allowed delineation of the interacting regions of the 3 integrin subunit and tetraspanin. In CD151, the sequence between residues Leu149 and Glu213 within the second half of the LECL is necessary and sufficient to confer stable association with 3ß1 integrin (Yauch et al., 2000; Berditchevski et al., 2001). This region includes all six cysteine residues present in the CD151 LECL, and mutation of the consecutive cysteine residues in the conserved CCG and PxxCC motifs precludes the direct association of CD151 with the integrin (Berditchevski et al., 2001). Hence, rather than being defined by a short linear sequence, the integrin-binding surface of CD151 is likely to be formed by various parts of the Leu149-Glu213 region, whose ternary fold is supported by the cysteine residues. It is not known whether this part of the CD151 LECL is also required for stabilisation of the CD151-6ß1 complex. The CD151 LECL is not required for the heterotypic CD151-tetraspanin interactions, however, and, therefore, cannot be responsible for bringing more distal tetraspanins to the CD151-3ß1 complex (Berditchevski et al., 2001).
Given the crucial role of the LECL in the CD151-3ß1 interaction, it is not surprising that the tetraspanin-binding site has been mapped to the extracellular portion of the 3 integrin subunit (Yauch et al., 1998; Yauch et al., 2000). Accordingly, substitution of the transmembrane and cytoplasmic domains of the 3 subunit with the corresponding regions of 5 does not affect its association with tetraspanins (Yauch et al., 1998). Using inter-integrin chimeras, Yauch and co-workers showed that part of the ‘stalk’ region within the 3 extracellular domain (the sequence between residues 569-705) is required for stable association with CD151 (Yauch et al., 2000). Although the interaction between 4ß1 and the tetraspanin CD81 has not been examined in detail, an early study established that mutation of two metal-binding sites in the 4 integrin subunit diminished the stability of the complex (Mannion et al., 1996). Notably, corresponding mutations in 3 did not affect the association with CD151 (Yauch et al., 2000), which suggests that the interacting interfaces of the CD151-3ß1 and CD81-4ß1 complexes differ. Interestingly, homology modelling predicts that the 3ß1-interacting part of CD151 and the corresponding region of CD81 have different folds (Seigneuret et al., 2001).
A conformational change in integrin receptors is an important mechanism for controlling their ligand-binding activity (Humphries, 2000; Plow et al., 2000). As yet, there is no evidence demonstrating that their association with tetraspanins influences integrin conformation. Neither is there any indication that a particular conformational state favours the association of integrins with tetraspanins. The results of numerous studies indicate that various integrin-tetraspanin complexes can be immunoprecipitated equally well regardless of whether function-blocking, neutral or function-activating anti-integrin antibodies are used. Divalent cations, which activate (or inhibit) the ligand-binding function of integrins (e.g. Mg2+, Mn2+ and Ca2+), have no effect on integrin association with tetraspanins (Longhurst et al., 1999; Mannion et al., 1996; Yáñez-Mó et al., 2001a). Finally, ligand binding does not seem to influence the stability of various integrin-tetraspanin complexes (Israels et al., 2001; Longhurst et al., 1999; Yáñez-Mó et al., 2001a).
An interesting aspect of the integrin-tetraspanin complex formation has been described recently: Ono and co-workers found that the association of CD82 with 3ß1 and 5ß1 depends on the glycosylation state of both tetraspanin and integrins (Ono et al., 2000). Given that the degree of CD82 glycosylation varies in different cell types (White et al., 1998), this may represent a tissue-specific control mechanism that regulates the assembly of the CD82-3ß1 and CD82-5ß1 complexes.
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The role of tetraspanins in integrin-mediated cell adhesion and migration |
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TopSUMMARYIntroductionThe structural basis for...The role of tetraspanins...Signal transduction by integrin...The role of tetraspanins...Integrin-tetraspanin complexes...PerspectivesREFERENCES |
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In contrast, numerous reports describe the involvement of tetraspanins in both homotypic and heterotypic cell-cell adhesion (Barrett et al., 1991; Bradbury et al., 1992; Cao et al., 1997; Fitter et al., 1999; Lazo et al., 1997; Lagaudriere-Gesbert et al., 1997; Letarte et al., 1993; Masellis-Smith et al., 1990; Schick and Levy, 1993; Shibagaki et al., 1998; Skubitz et al., 1996; Toothill et al., 1990). The possible involvement of tetraspanins in intercellular adhesion has been a focus of a recent review (Yáñez-Mó et al., 2001b). It has to be emphasised that intercellular contacts are controlled by a diverse range of receptor-ligand interactions in which integrins play either a major (as in hematopoetic cells) or an auxiliary role. Given that tetraspanins can form complexes with various other transmembrane proteins, their role in regulating intercellular contacts may also involve non-integrin adhesion receptors (Lazo et al., 1997).
The involvement of tetraspanins in cell motility is well documented. Numerous reports published over the past ten years have demonstrated that tetraspanins are implicated in migration of monolayers (e.g. in wound closure), as well as in the random and chemotactic motility of various cell types (Ikeyama et al., 1993; Klein-Soyer et al., 2000; Miyake et al., 1991; Ono et al., 2000; Penas et al., 2000; Radford et al., 1997; Shaw et al., 1995; Sincock et al., 1999; Yáñez-Mó et al., 1998; Yáñez-Mó et al., 2001a). In addition, recent data indicate that tetraspanins are involved in more complex biological phenomena driven by integrin-ECM interactions. These include invasive migration of carcinoma cells within the 3D ECM (Sugiura and Berditchevski, 1999), collagen-gel contraction (Scherberich et al., 1998), morphogenetic re-organisation of monolayers of epithelial cells (Yáñez-Mó et al., 2001a) and neurite outgrowth (Stipp and Hemler, 2000).
Cell migration is a complex phenomenon that is controlled by highly regulated processes both at the leading edge and at the rear of the cell (Lauffenburger and Horwitz, 1996). In both stationary and migratory cells, tetraspanin-containing protein complexes are highly abundant at the outermost cell periphery (Berditchevski and Odintsova, 1999; Berditchevski et al., 1997b). These highly dynamic parts of the cell are engaged in transient interactions with the substrate and trigger the initial set of biochemical signals that leads to the assembly of more stable attachment structures (e.g. focal adhesions). Two recent reports indicate that tetraspanin-containing adhesion complexes may control the protrusion activity in migrating cells. Firstly, antibody-interference experiments have demonstrated that in keratinocytes, tetraspanins regulate lamellipodia formation (Baudoux et al., 2000). Secondly, elongation of the invasive protrusions of breast carcinoma cells embedded into the 3D ECM can be stimulated by antibodies to various tetraspanins and the 3 integrin subunit (Sugiura and Berditchevski, 1999). Detailed time-lapse analysis has shown that antibody treatment attenuates retraction of the extending protrusions (Sugiura and Berditchevski, 1999).
Current data suggest that the pro- or anti-migratory activities of tetraspanins are not limited to a particular ECM ligand (Shaw et al., 1995, Domanico et al., 1997). Furthermore, binding of the tetraspanins can affect integrin-mediated cell migration in both a ligand-dependent and a ligand-independent fashion (Domanico et al., 1997). In most cells, the tetraspanin-containing peripheral adhesion complexes are devoid of cytoskeletal and signalling components typically found in more stable adhesion structures, such as focal adhesions and Rac-dependent focal complexes (e.g. vinculin, paxilin and FAK) (Berditchevski and Odintsova, 1999; Penas et al., 2000). In contrast, tetraspanins are colocalised with MARCKS (myristoylated alanine-rich C kinase substrate), one of the prominent substrates for different members of the protein kinase C (PKC) family (Berditchevski and Odintsova, 1999). One of the proposed functions of MARCKS is regulation of cortical cytoskeleton dynamics during cell spreading and migration (Wiederkehr et al., 1997). Given that certain tetraspanins can associate with PKC enzymes (Zhang, et al., 2001a), it is conceivable that the tetraspanin-containing adhesion complexes affect the actin-reorganising activity of MARCKS.
In sections of normal skin and cultured keratinocytes, the anti-CD151 antibody (but not several other anti-tetraspanin antibodies) label hemidesmosomes – specialised junctional complexes that mediate stable attachment of cells to the basement membrane (Sterk et al., 2000). Thus, CD151 might have opposing functions in cell migration: in non-transformed epithelial cells, it could be involved in the stabilization of cell attachment, but in carcinomas, the elevated expression of CD151 potentiates their pro-migratory phenotype (Testa et al., 1999).
Finally, in some cells (epithelia and endothelia), integrin-tetraspanin complexes are enriched at cell-cell contact sites (Nakamura et al., 1995; Penas et al., 2000; Yáñez-Mó et al., 2001b), where they may affect migration indirectly by regulating the dynamics of intercellular communication.
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Signal transduction by integrin-tetraspanin protein complexes |
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TopSUMMARYIntroductionThe structural basis for...The role of tetraspanins...Signal transduction by integrin...The role of tetraspanins...Integrin-tetraspanin complexes...PerspectivesREFERENCES |
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4ß1 and 6ß1 integrins and potentiates fibronectin- and laminin-1-dependent tyrosine phosphorylation of 130 kDa and 69 kDa proteins (Shaw et al., 1995). In addition, expression of CD9 in fibrosarcoma cells specifically affects the de-phosphorylation rate of FAK (Berditchevski and Odintsova, 1999), and clustering of the 3ß1-tetraspanin complexes in breast carcinoma cells stimulates the PI3-kinase-dependent signalling pathway (Sugiura and Berditchevski, 1999).
The contribution of tetraspanins to adhesion-dependent signalling might be linked with their ability to recruit certain signalling enzymes into the integrin complexes (Hemler, 1998). A number of tetraspanins, including CD9, CD63, CD81, A15/Talla-1 and CD151 (but not CD82, CD37, CD53 or NAG-2/Tspan-4), are associated with type II phosphatidylinositol 4-kinase (PtdIns 4-K), one of the key enzymes in synthesis of C-4 phosphoinositides (Berditchevski et al., 1997b; Yauch and Hemler, 2000). Furthermore, the association with CD151 seems to be critical for tethering of PtdIns 4-K to 3ß1 integrin (Yauch and Hemler, 2000). Given the lack of apparent similarity between the cytoplasmic portions of the PtdIns 4-K-linked tetraspanins, the association is probably mediated by another part(s) of the protein. Although the interaction of PtdIns 4-K with tetraspanins does not require their association with integrins, not all tetraspanin-linked integrins (e.g. 4ß1 and 6ß1) are associated with the PtdIns 4-K activity (Yauch and Hemler, 2000). This suggests that additional mechanisms (or protein components) that control the association of the enzyme with integrins exist. Whether or not binding of the 3ß1 integrin to ECM ligands regulates the activity of the enzyme within the complex is not known.
Treatment of cells with phorbol ester (PMA) induces association of various tetraspanins (e.g. CD9, CD53, CD81, CD82 and CD151) with two members of the PKC family, and ßII (Zhang et al., 2001a). The specificity of the tetraspanin-PKC interaction is further strengthened by the fact that other PKC enzymes, including PKC
, PKC
and PKCµ, are not associated with the tetraspanin complexes (Zhang et al., 2001a). An interaction with integrins is not required for the association of tetraspanins with PKC, which suggests that tetraspanins play a critical role in recruiting PKC into the integrin complexes (3ß1 and 6ß1). Furthermore, PKC-dependent phosphorylation of the 3 integrin subunit is critical for cell migration and for the adhesion-dependent signalling mediated by 3ß1 (Zhang et al., 2001b).
Two Src family tyrosine kinases, Lyn and Hck, and unspecified serine/threonine kinase activities, are associated with the ß2-integrin–CD63 complex and might play an important role in the CD63-induced upregulation and activation of ß2 integrins in human neutrophils (Skubitz et al., 1996).
The ability to associate simultaneously with one another and various classes of transmembrane proteins might mean that tetraspanins can transmit lateral signals between integrins and other surface receptors. This could further diversify the contribution of tetraspanin proteins to adhesion-dependent signalling. For example, in B cells, the network of tetraspanins may juxtapose 4ß1 and 5ß1 integrins with the CD21-CD19-Leu13 complex, so that antibody-induced crosslinking of integrins or tetraspanins induces phosphorylation of CD19 (Horvath et al., 1998; Xiao et al., 1996). Conversely, clustering of CD19 complexes induces tyrosine-kinase-dependent adhesion of B cells to cell-deposited fibronectin, a process mediated by 4ß1 integrin (Behr and Schriever, 1995).
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The role of tetraspanins in integrin maturation and trafficking |
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TopSUMMARYIntroductionThe structural basis for...The role of tetraspanins...Signal transduction by integrin...The role of tetraspanins...Integrin-tetraspanin complexes...PerspectivesREFERENCES |
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3ß1-integrin–tetraspanin complexes: the interaction with CD151 takes place early during integrin biosynthesis – the association of CD151 with the pre-3 subunit is detectable even before the ß1 subunit joins the complex (Berditchevski et al., 2001). Furthermore, CD151 mutants that are sequestered in the endoplasmic reticulum (ER) retain their ability to associate with 3ß1 (Berditchevski et al., 2001). In contrast, other tetraspanins, including CD9, CD63 and CD81, are associated only with the mature heterodimer. In cells that have an abundant pool of intracellular integrins, CD9 (but not CD81 or CD82) is associated with the pre-ß1 subunit and calnexin, an ER chaperone protein (Rubinstein et al., 1997). Whether or not these early associations with tetraspanins are required for proper biogenesis of the integrin heterodimers remains to be determined.
Immunoelectron microscopy and immunofluorescence studies have demonstrated that tetraspanins are abundant on various types of intracellular vesicles (Escola et al., 1998; Hamamoto et al., 1994; Hotchin et al., 1995; Peters et al., 1991; Sincock et al., 1999). These data point to a possible role for tetraspanins in turnover and/or sorting of integrins. Several tetraspanins contain a tyrosine-based sorting motif (Tyr-X-X-
) at their C-termini (Table 2) that might recruit clathrin adapter proteins to the integrin complexes and thereby direct them along various trafficking routes (Bonifacino and Dell’Angelica, 1999). The tetraspanin-associated PtdIns 4-K and PKC can also contribute to this ‘sorting’ function of tetraspanins (Fig. 2). Indeed, activation of PKC in mammary epithelial cells facilitates internalisation of ß1 integrins (Ng et al., 1999).
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Integrin-tetraspanin complexes and lipid rafts |
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TopSUMMARYIntroductionThe structural basis for...The role of tetraspanins...Signal transduction by integrin...The role of tetraspanins...Integrin-tetraspanin complexes...PerspectivesREFERENCES |
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IIbß3 integrin are co-fractionated with the protein components of lipid rafts in low-density fractions in a sucrose gradient (Dorahy et al., 1996). More recently, the same has been shown to occur for other tetraspanins (e.g. CD9, CD63, CD81, CD82 and CD151) and integrins (3ß1 and Lß2) (Claas et al., 2001; Odintsova et al., 2000; Skubitz et al., 2000). Furthermore, tetraspanins are partially colocalised with the ganglioside GM1, a marker for lipid rafts (Claas et al., 2001). However, both biochemical (sucrose gradient fractionation) and immunofluorescence (colocalisation with GPI-linked proteins) experiments clearly indicate that a significant proportion of the integrin-tetraspanin protein complexes reside outside lipid rafts (Berditchevski et al., 1996; Claas et al., 2001; Dorahy et al., 1996). Thus, it has been proposed that the tetraspanin-enriched membrane patches may represent a new class of membrane microdomain that differs from conventional rafts (Claas et al., 2001). Furthermore, a non-uniform distribution could reflect either structural and, possibly, functional heterogeneity of the complexes or their lateral dynamics in the plasma membrane. It is also possible that integrin-tetraspanin complexes shuttle in and out of rafts and thereby control the recruitment of other proteins into these compartments (Claas et al., 2001). This function may be facilitated by fatty acyl groups that are covalently linked to tetraspanins (Seehafer et al., 1988; Seehafer et al., 1990). |
Perspectives |
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TopSUMMARYIntroductionThe structural basis for...The role of tetraspanins...Signal transduction by integrin...The role of tetraspanins...Integrin-tetraspanin complexes...PerspectivesREFERENCES |
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3ß1-CD151 interaction also form the contact interface of other integrin-tetraspanin pairs. Furthermore, what is the hierarchical order of the interactions between integrin-proximal CD151-CD81 and other tetraspanins? A detailed pair-wise analysis of various tetraspanin-tetraspanin interactions should determine the spatial organisation of integrin-tetraspanin clusters and set up a structural framework for future functional analyses. An important aspect of this work will be to establish which part(s) of tetraspanins controls their association with PtdIns 4-K and PKC isoforms. Current data pose a number of intriguing questions for the future. Firstly, why is PtdIns 4-K-associated activity not detected in the 6ß1-tetraspanin and 4ß1-tetraspanin complexes (Yauch et al., 1998)? Are there integrin-specific exclusion/inhibitory mechanisms? A comprehensive biochemical dissection of integrin-tetraspanin complexes and extensive mutagenesis of their components should answer these questions. Furthermore, what are the physiological pathways that regulate the association of PtdIns 4-K and PKC with the complexes and their activities? Early reports indicated that the activity of PtdIns-K is upregulated in cells treated with EGF (Kauffmann-Zeh et al., 1994). Does EGF also affect the activity of the enzyme associated with the integrin-tetraspanin complex? Do tetraspanins, which are known to associate with the EGF receptor (Odintsova et al., 2000), facilitate this process? Many physiological stimuli are known to activate PKC, which, in turn, may affect both adhesive and non-adhesive properties of integrins, including their clustering, post-ligand binding signalling, and turnover. It will be important to identify those stimuli that are specifically directed towards the isoforms of PKC associated with tetraspanin complexes. Such detailed dissection of both lateral and vertical ‘signalling waves’ involving tetraspanins should answer an important outstanding question – whether tetraspanins function as a combined signalling entity (e.g. as components of the ‘tetraspanin web’) or whether each of the integrin-tetraspanin complexes makes its own specific contribution to adhesion-dependent signalling.
The function of tetraspanins is clearly important in integrin-driven cell migration. Given the distinct composition of integrin-tetraspanin adhesion complexes, it will be crucial to identify specific proximal targets for the activated integrin-tetraspanin complexes. Tetraspanin-associated PtdIns 4-K can enhance synthesis of phosphoinositides in proximity to integrins (Fig. 2). This may affect the actin-binding properties of a number of integrin-associated cytoskeletal proteins (e.g. -actinin, talin and filamin). Alternatively, locally generated phosphoinositides may function as anchors for the recruitment of cytoplasmic proteins (e.g. MARCKS) into the integrin vicinity (Fig. 2). Similarly, the activity of the tetraspanin-associated PKC may be directed towards various protein targets (both cytoskeletal and signalling). Identification of new components within integrin-tetraspanin complexes and studying their involvement in PKC-dependent signalling should become a focus of future experiments. Another important aspect of future work will be to examine the spatial dynamics of the complexes in migrating cells, particularly in relation to cytoskeleton and adhesion-related signalling proteins. These experiments should place tetraspanin-dependent processes into a specific signalling context and answer the question of whether there is a functional link between tetraspanin-containing adhesion complexes and the more stable focal adhesions.
It is currently recognised that targeted delivery of integrins to the leading edge of migrating cells and their recycling may help to perpetuate lamellipodial extensions (Fabbri et al., 1999; Lauffenburger and Horwitz, 1996; Pierini et al., 2000). Certainly, the occurrence of the tyrosine-based sorting signal in some tetraspanins equips them with the potential to serve as navigators that direct integrin trafficking during the migration. A comparative real-time analysis of integrin trafficking in cells expressing tetraspanins in which the sorting signal is obliterated should establish whether this potential is indeed realised.
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ACKNOWLEDGMENTS |
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Footnotes |
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The LECLs of the tetraspanins rom-1 and RDS have an additional cysteine, which precedes the CCG-sequence (Bascom et al., 1992; Travis et al., 1989). The LECL of Tspan-5 has an additional pair of cysteines (Todd et al., 1998).
* Some of the discrepancies observed in the literature may reflect differences in the purification conditions used in the immunoprecipitation experiments.
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TopSUMMARYIntroductionThe structural basis for...The role of tetraspanins...Signal transduction by integrin...The role of tetraspanins...Integrin-tetraspanin complexes...PerspectivesREFERENCES |
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 S. Kuhn, M. Koch, T. Nubel, M. Ladwein, D. Antolovic, P. Klingbeil, D. Hildebrand, G. Moldenhauer, L. Langbein, W. W. Franke, et al. A Complex of EpCAM, Claudin-7, CD44 Variant Isoforms, and Tetraspanins Promotes Colorectal Cancer Progression Mol. Cancer Res., June 1, 2007; 5(6): 553 - 567. [Abstract] [Full Text] [PDF]
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Y. Takeda, A. R. Kazarov, C. E. Butterfield, B. D. Hopkins, L. E. Benjamin, A. Kaipainen, and M. E. Hemler Deletion of tetraspanin Cd151 results in decreased pathologic angiogenesis in vivo and in vitro Blood, February 15, 2007; 109(4): 1524 - 1532. [Abstract] [Full Text] [PDF]
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D. Mazurov, G. Heidecker, and D. Derse The Inner Loop of Tetraspanins CD82 and CD81 Mediates Interactions with Human T Cell Lymphotrophic Virus Type 1 Gag Protein J. Biol. Chem., February 9, 2007; 282(6): 3896 - 3903. [Abstract] [Full Text] [PDF]
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T. Isaji, Y. Sato, Y. Zhao, E. Miyoshi, Y. Wada, N. Taniguchi, and J. Gu N-Glycosylation of the beta-Propeller Domain of the Integrin {alpha}5 Subunit Is Essential for {alpha}5beta1 Heterodimerization, Expression on the Cell Surface, and Its Biological Function J. Biol. Chem., November 3, 2006; 281(44): 33258 - 33267. [Abstract] [Full Text] [PDF]
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 S.-a. Ha, M. Tsuji, K. Suzuki, B. Meek, N. Yasuda, T. Kaisho, and S. Fagarasan Regulation of B1 cell migration by signals through Toll-like receptors J. Exp. Med., October 30, 2006; 203(11): 2541 - 2550. [Abstract] [Full Text] [PDF]
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 M. Gordon-Alonso, M. Yanez-Mo, O. Barreiro, S. Alvarez, M. A. Munoz-Fernandez, A. Valenzuela-Fernandez, and F. Sanchez-Madrid Tetraspanins CD9 and CD81 Modulate HIV-1-Induced Membrane Fusion J. Immunol., October 15, 2006; 177(8): 5129 - 5137. [Abstract] [Full Text] [PDF]
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M. W. Goschnick, L.-M. Lau, J. L. Wee, Y. S. Liu, P. M. Hogarth, L. M. Robb, M. J. Hickey, M. D. Wright, and D. E. Jackson Impaired "outside-in" integrin {alpha}IIbbeta3 signaling and thrombus stability in TSSC6-deficient mice Blood, September 15, 2006; 108(6): 1911 - 1918. [Abstract] [Full Text] [PDF]
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I.-K. Hong, Y.-J. Jin, H.-J. Byun, D.-I. Jeoung, Y.-M. Kim, and H. Lee Homophilic Interactions of Tetraspanin CD151 Up-regulate Motility and Matrix Metalloproteinase-9 Expression of Human Melanoma Cells through Adhesion-dependent c-Jun Activation Signaling Pathways J. Biol. Chem., August 25, 2006; 281(34): 24279 - 24292. [Abstract] [Full Text] [PDF]
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S. Gesierich, I. Berezovskiy, E. Ryschich, and M. Zoller Systemic Induction of the Angiogenesis Switch by the Tetraspanin D6.1A/CO-029. Cancer Res., July 15, 2006; 66(14): 7083 - 7094. [Abstract] [Full Text] [PDF]
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M. Sala-Valdes, A. Ursa, S. Charrin, E. Rubinstein, M. E. Hemler, F. Sanchez-Madrid, and M. Yanez-Mo EWI-2 and EWI-F Link the Tetraspanin Web to the Actin Cytoskeleton through Their Direct Association with Ezrin-Radixin-Moesin Proteins J. Biol. Chem., July 14, 2006; 281(28): 19665 - 19675. [Abstract] [Full Text] [PDF]
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 H. Ohtsu, P. J. Dempsey, and S. Eguchi ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors Am J Physiol Cell Physiol, July 1, 2006; 291(1): C1 - C10. [Abstract] [Full Text] [PDF]
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 T.-T. Sun Altered phenotype of cultured urothelial and other stratified epithelial cells: implications for wound healing Am J Physiol Renal Physiol, July 1, 2006; 291(1): F9 - F21. [Abstract] [Full Text] [PDF]
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G. Min, H. Wang, T.-T. Sun, and X.-P. Kong Structural basis for tetraspanin functions as revealed by the cryo-EM structure of uroplakin complexes at 6-A resolution J. Cell Biol., June 19, 2006; 173(6): 975 - 983. [Abstract] [Full Text] [PDF]
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S. Nydegger, S. Khurana, D. N. Krementsov, M. Foti, and M. Thali Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1 J. Cell Biol., June 5, 2006; 173(5): 795 - 807. [Abstract] [Full Text] [PDF]
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N. E. Winterwood, A. Varzavand, M. N. Meland, L. K. Ashman, and C. S. Stipp A Critical Role for Tetraspanin CD151 in {alpha}3beta1 and {alpha}6beta4 Integrin-dependent Tumor Cell Functions on Laminin-5 Mol. Biol. Cell, June 1, 2006; 17(6): 2707 - 2721. [Abstract] [Full Text] [PDF]
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X. H. Yang, O. V. Kovalenko, T. V. Kolesnikova, M. M. Andzelm, E. Rubinstein, J. L. Strominger, and M. E. Hemler Contrasting Effects of EWI Proteins, Integrins, and Protein Palmitoylation on Cell Surface CD9 Organization J. Biol. Chem., May 5, 2006; 281(18): 12976 - 12985. [Abstract] [Full Text] [PDF]
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C. Bertaux and T. Dragic Different domains of CD81 mediate distinct stages of hepatitis C virus pseudoparticle entry. J. Virol., May 1, 2006; 80(10): 4940 - 4948. [Abstract] [Full Text] [PDF]
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A. Ziyyat, E. Rubinstein, F. Monier-Gavelle, V. Barraud, O. Kulski, M. Prenant, C. Boucheix, M. Bomsel, and J.-P. Wolf CD9 controls the formation of clusters that contain tetraspanins and the integrin {alpha}6{beta}1, which are involved in human and mouse gamete fusion J. Cell Sci., February 1, 2006; 119(3): 416 - 424. [Abstract] [Full Text] [PDF]
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 A. Ziyyat, N. Naud-Barriant, V. Barraud-Lange, F. Chevalier, O. Kulski, T. Lemkecher, M. Bomsel, and J.P. Wolf Cyclic FEE peptide increases human gamete fusion and potentiates its RGD-induced inhibition Hum. Reprod., December 1, 2005; 20(12): 3452 - 3458. [Abstract] [Full Text] [PDF]
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M.-T. Zilber, N. Setterblad, T. Vasselon, C. Doliger, D. Charron, N. Mooney, and C. Gelin MHC class II/CD38/CD9: a lipid-raft-dependent signaling complex in human monocytes Blood, November 1, 2005; 106(9): 3074 - 3081. [Abstract] [Full Text] [PDF]
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F. Martin, D. M. Roth, D. A. Jans, C. W. Pouton, L. J. Partridge, P. N. Monk, and G. W. Moseley Tetraspanins in Viral Infections: a Fundamental Role in Viral Biology? J. Virol., September 1, 2005; 79(17): 10839 - 10851. [Full Text] [PDF]
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 S. Levy and T. Shoham Protein-Protein Interactions in the Tetraspanin Web Physiology, August 1, 2005; 20(4): 218 - 224. [Abstract] [Full Text] [PDF]
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 F. Dominguez, M. Yanez-Mo, F. Sanchez-Madrid, and C. Simon Embryonic implantation and leukocyte transendothelial migration: different processes with similar players? FASEB J, July 1, 2005; 19(9): 1056 - 1060. [Abstract] [Full Text] [PDF]
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H. Huang, J. Groth, K. Sossey-Alaoui, L. Hawthorn, S. Beall, and J. Geradts Aberrant Expression of Novel and Previously Described Cell Membrane Markers in Human Breast Cancer Cell Lines and Tumors Clin. Cancer Res., June 15, 2005; 11(12): 4357 - 4364. [Abstract] [Full Text] [PDF]
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E. C. Seales, G. A. Jurado, B. A. Brunson, J. K. Wakefield, A. R. Frost, and S. L. Bellis Hypersialylation of {beta}1 Integrins, Observed in Colon Adenocarcinoma, May Contribute to Cancer Progression by Up-regulating Cell Motility Cancer Res., June 1, 2005; 65(11): 4645 - 4652. [Abstract] [Full Text] [PDF]
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R. Bass, F. Werner, E. Odintsova, T. Sugiura, F. Berditchevski, and V. Ellis Regulation of Urokinase Receptor Proteolytic Function by the Tetraspanin CD82 J. Biol. Chem., April 15, 2005; 280(15): 14811 - 14818. [Abstract] [Full Text] [PDF]
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S. Gesierich, C. Paret, D. Hildebrand, J. Weitz, K. Zgraggen, F. H. Schmitz-Winnenthal, V. Horejsi, O. Yoshie, D. Herlyn, L. K. Ashman, et al. Colocalization of the Tetraspanins, CO-029 and CD151, with Integrins in Human Pancreatic Adenocarcinoma: Impact on Cell Motility Clin. Cancer Res., April 15, 2005; 11(8): 2840 - 2852. [Abstract] [Full Text] [PDF]
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M. Furuya, H. Kato, N. Nishimura, I. Ishiwata, H. Ikeda, R. Ito, T. Yoshiki, and H. Ishikura Down-regulation of CD9 in Human Ovarian Carcinoma Cell Might Contribute to Peritoneal Dissemination: Morphologic Alteration and Reduced Expression of {beta}1 Integrin Subsets Cancer Res., April 1, 2005; 65(7): 2617 - 2625. [Abstract] [Full Text] [PDF]
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O. Barreiro, M. Yanez-Mo, M. Sala-Valdes, M. D. Gutierrez-Lopez, S. Ovalle, A. Higginbottom, P. N. Monk, C. Cabanas, and F. Sanchez-Madrid Endothelial tetraspanin microdomains regulate leukocyte firm adhesion during extravasation Blood, April 1, 2005; 105(7): 2852 - 2861. [Abstract] [Full Text] [PDF]
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M. Damek-Poprawa, J. Krouse, C. Gretzula, and K. Boesze-Battaglia A Novel Tetraspanin Fusion Protein, Peripherin-2, Requires a Region Upstream of the Fusion Domain for Activity J. Biol. Chem., March 11, 2005; 280(10): 9217 - 9224. [Abstract] [Full Text] [PDF]
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R. B. Irby, R. L. Malek, G. Bloom, J. Tsai, N. Letwin, B. C. Frank, K. Verratti, T. J. Yeatman, and N. H. Lee Iterative Microarray and RNA Interference-Based Interrogation of the Src-Induced Invasive Phenotype Cancer Res., March 1, 2005; 65(5): 1814 - 1821. [Abstract] [Full Text] [PDF]
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S. Bodin, C. Soulet, H. Tronchere, P. Sie, C. Gachet, M. Plantavid, and B. Payrastre Integrin-dependent interaction of lipid rafts with the actin cytoskeleton in activated human platelets J. Cell Sci., February 15, 2005; 118(4): 759 - 769. [Abstract] [Full Text] [PDF]
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J. Lu, K. I. Izvolsky, J. Qian, and W. V. Cardoso Identification of FGF10 Targets in the Embryonic Lung Epithelium during Bud Morphogenesis J. Biol. Chem., February 11, 2005; 280(6): 4834 - 4841. [Abstract] [Full Text] [PDF]
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S. Kraft, T. Fleming, J. M. Billingsley, S.-Y. Lin, M.-H. Jouvin, P. Storz, and J.-P. Kinet Anti-CD63 antibodies suppress IgE-dependent allergic reactions in vitro and in vivo J. Exp. Med., February 7, 2005; 201(3): 385 - 396. [Abstract] [Full Text] [PDF]
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B. He, L. Liu, G. A. Cook, S. Grgurevich, L. K. Jennings, and X. A. Zhang Tetraspanin CD82 Attenuates Cellular Morphogenesis through Down-regulating Integrin {alpha}6-Mediated Cell Adhesion J. Biol. Chem., February 4, 2005; 280(5): 3346 - 3354. [Abstract] [Full Text] [PDF]
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 J. J. Lepore, T. P. Cappola, P. A. Mericko, E. E. Morrisey, and M. S. Parmacek GATA-6 Regulates Genes Promoting Synthetic Functions in Vascular Smooth Muscle Cells Arterioscler. Thromb. Vasc. Biol., February 1, 2005; 25(2): 309 - 314. [Abstract] [Full Text] [PDF]
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X.-T. Kong, F.-M. Deng, P. Hu, F.-X. Liang, G. Zhou, A. B. Auerbach, N. Genieser, P. K. Nelson, E. S. Robbins, E. Shapiro, et al. Roles of uroplakins in plaque formation, umbrella cell enlargement, and urinary tract diseases J. Cell Biol., December 20, 2004; 167(6): 1195 - 1204. [Abstract] [Full Text] [PDF]
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X. Yang, O. V. Kovalenko, W. Tang, C. Claas, C. S. Stipp, and M. E. Hemler Palmitoylation supports assembly and function of integrin-tetraspanin complexes J. Cell Biol., December 20, 2004; 167(6): 1231 - 1240. [Abstract] [Full Text] [PDF]
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 J. Renshaw, R. M. Orr, M. I. Walton, R. te Poele, R. D. Williams, E. V. Wancewicz, B. P. Monia, P. Workman, and K. Pritchard-Jones Disruption of WT1 gene expression and exon 5 splicing following cytotoxic drug treatment: Antisense down-regulation of exon 5 alters target gene expression and inhibits cell survival Mol. Cancer Ther., November 1, 2004; 3(11): 1467 - 1484. [Abstract] [Full Text] [PDF]
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B. Zhou, L. Liu, M. Reddivari, and X. A. Zhang The Palmitoylation of Metastasis Suppressor KAI1/CD82 Is Important for Its Motility- and Invasiveness-Inhibitory Activity Cancer Res., October 15, 2004; 64(20): 7455 - 7463. [Abstract] [Full Text] [PDF]
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D. Baronas-Lowell, J. L. Lauer-Fields, J. A. Borgia, G. F. Sferrazza, M. Al-Ghoul, D. Minond, and G. B. Fields Differential Modulation of Human Melanoma Cell Metalloproteinase Expression by {alpha}2{beta}1 Integrin and CD44 Triple-helical Ligands Derived from Type IV Collagen J. Biol. Chem., October 15, 2004; 279(42): 43503 - 43513. [Abstract] [Full Text] [PDF]
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A. Delaguillaumie, J. Harriague, S. Kohanna, G. Bismuth, E. Rubinstein, M. Seigneuret, and H. Conjeaud Tetraspanin CD82 controls the association of cholesterol-dependent microdomains with the actin cytoskeleton in T lymphocytes: relevance to co-stimulation J. Cell Sci., October 15, 2004; 117(22): 5269 - 5282. [Abstract] [Full Text] [PDF]
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H. Moribe, J. Yochem, H. Yamada, Y. Tabuse, T. Fujimoto, and E. Mekada Tetraspanin protein (TSP-15) is required for epidermal integrity in Caenorhabditis elegans J. Cell Sci., October 15, 2004; 117(22): 5209 - 5220. [Abstract] [Full Text] [PDF]
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V. Karamatic Crew, N. Burton, A. Kagan, C. A. Green, C. Levene, F. Flinter, R. L. Brady, G. Daniels, and D. J. Anstee CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin Blood, October 15, 2004; 104(8): 2217 - 2223. [Abstract] [Full Text] [PDF]
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L.-M. Lau, J. L. Wee, M. D. Wright, G. W. Moseley, P. M. Hogarth, L. K. Ashman, and D. E. Jackson The tetraspanin superfamily member CD151 regulates outside-in integrin {alpha}IIb{beta}3 signaling and platelet function Blood, October 15, 2004; 104(8): 2368 - 2375. [Abstract] [Full Text] [PDF]
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 D. D. Mruk and C. Y. Cheng Sertoli-Sertoli and Sertoli-Germ Cell Interactions and Their Significance in Germ Cell Movement in the Seminiferous Epithelium during Spermatogenesis Endocr. Rev., October 1, 2004; 25(5): 747 - 806. [Abstract] [Full Text] [PDF]
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F. Magnani, C. G. Tate, S. Wynne, C. Williams, and J. Haase Partitioning of the Serotonin Transporter into Lipid Microdomains Modulates Transport of Serotonin J. Biol. Chem., September 10, 2004; 279(37): 38770 - 38778. [Abstract] [Full Text] [PDF]
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 M. D. Wright, S. M. Geary, S. Fitter, G. W. Moseley, L.-M. Lau, K.-C. Sheng, V. Apostolopoulos, E. G. Stanley, D. E. Jackson, and L. K. Ashman Characterization of Mice Lacking the Tetraspanin Superfamily Member CD151 Mol. Cell. Biol., July 1, 2004; 24(13): 5978 - 5988. [Abstract] [Full Text] [PDF]
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Y. Murayama, J.-i. Miyagawa, K. Oritani, H. Yoshida, K. Yamamoto, O. Kishida, T. Miyazaki, S. Tsutsui, T. Kiyohara, Y. Miyazaki, et al. CD9-mediated activation of the p46 Shc isoform leads to apoptosis in cancer cells J. Cell Sci., July 1, 2004; 117(15): 3379 - 3388. [Abstract] [Full Text] [PDF]
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M. Wadehra, L. Goodglick, and J. Braun The Tetraspan Protein EMP2 Modulates the Surface Expression of Caveolins and Glycosylphosphatidyl Inositol-linked Proteins Mol. Biol. Cell, May 1, 2004; 15(5): 2073 - 2083. [Abstract] [Full Text] [PDF]
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K. D. Little, M. E. Hemler, and C. S. Stipp Dynamic Regulation of a GPCR-Tetraspanin-G Protein Complex on Intact Cells: Central Role of CD81 in Facilitating GPR56-G{alpha}q/11 Association Mol. Biol. Cell, May 1, 2004; 15(5): 2375 - 2387. [Abstract] [Full Text] [PDF]
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M. Cortes-Canteli, M. Wagner, W. Ansorge, and A. Perez-Castillo Microarray Analysis Supports a Role for CCAAT/Enhancer-binding Protein-{beta} in Brain Injury J. Biol. Chem., April 2, 2004; 279(14): 14409 - 14417. [Abstract] [Full Text] [PDF]
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A. B. van Spriel, K. L. Puls, M. Sofi, D. Pouniotis, H. Hochrein, Z. Orinska, K.-P. Knobeloch, M. Plebanski, and M. D. Wright A Regulatory Role for CD37 in T Cell Proliferation J. Immunol., March 1, 2004; 172(5): 2953 - 2961. [Abstract] [Full Text] [PDF]
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 Y.-H. Li, Y. Hou, W. Ma, J.-X. Yuan, D. Zhang, Q.-Y. Sun, and W.-H. Wang Localization of CD9 in pig oocytes and its effects on sperm-egg interaction Reproduction, February 1, 2004; 127(2): 151 - 157. [Abstract] [Full Text] [PDF]
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 T. Ishibashi, L. Ding, K. Ikenaka, Y. Inoue, K. Miyado, E. Mekada, and H. Baba Tetraspanin Protein CD9 Is a Novel Paranodal Component Regulating Paranodal Junctional Formation J. Neurosci., January 7, 2004; 24(1): 96 - 102. [Abstract] [Full Text] [PDF]
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A. Cherukuri, T. Shoham, H. W. Sohn, S. Levy, S. Brooks, R. Carter, and S. K. Pierce The Tetraspanin CD81 Is Necessary for Partitioning of Coligated CD19/CD21-B Cell Antigen Receptor Complexes into Signaling-Active Lipid Rafts J. Immunol., January 1, 2004; 172(1): 370 - 380. [Abstract] [Full Text] [PDF]
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 A. Duffield, E.-J. Kamsteeg, A. N. Brown, P. Pagel, and M. J. Caplan The tetraspanin CD63 enhances the internalization of the H,K-ATPase {beta}-subunit PNAS, December 23, 2003; 100(26): 15560 - 15565. [Abstract] [Full Text] [PDF]
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N. Chattopadhyay, Z. Wang, L. K. Ashman, S. M. Brady-Kalnay, and J. A. Kreidberg {alpha}3{beta}1 integrin-CD151, a component of the cadherin-catenin complex, regulates PTP{micro} expression and cell-cell adhesion J. Cell Biol., December 22, 2003; 163(6): 1351 - 1362. [Abstract] [Full Text] [PDF]
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C. S. Stipp, T. V. Kolesnikova, and M. E. Hemler EWI-2 regulates {alpha}3{beta}1 integrin-dependent cell functions on laminin-5 J. Cell Biol., December 8, 2003; 163(5): 1167 - 1177. [Abstract] [Full Text] [PDF]
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 E. Ito, R. Honma, J.-i. Imai, S. Azuma, T. Kanno, S. Mori, O. Yoshie, J. Nishio, H. Iwasaki, K. Yoshida, et al. A Tetraspanin-Family Protein, T-Cell Acute Lymphoblastic Leukemia-Associated Antigen 1, Is Induced by the Ewing's Sarcoma-Wilms' Tumor 1 Fusion Protein of Desmoplastic Small Round-Cell Tumor Am. J. Pathol., December 1, 2003; 163(6): 2165 - 2172. [Abstract] [Full Text]
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H. J. Hathaway, S. C. Evans, D. H. Dubois, C. I. Foote, B. H. Elder, and B. D. Shur Mutational analysis of the cytoplasmic domain of {beta}1,4-galactosyltransferase I: influence of phosphorylation on cell surface expression J. Cell Sci., November 1, 2003; 116(21): 4319 - 4330. [Abstract] [Full Text] [PDF]
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 F. Baluska, J. Samaj, P. Wojtaszek, D. Volkmann, and D. Menzel Cytoskeleton-Plasma Membrane-Cell Wall Continuum in Plants. Emerging Links Revisited Plant Physiology, October 1, 2003; 133(2): 482 - 491. [Full Text] [PDF]
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P. Alberts, R. Rudge, I. Hinners, A. Muzerelle, S. Martinez-Arca, T. Irinopoulou, V. Marthiens, S. Tooze, F. Rathjen, P. Gaspar, et al. Cross Talk between Tetanus Neurotoxin-insensitive Vesicle-associated Membrane Protein-mediated Transport and L1-mediated Adhesion Mol. Biol. Cell, October 1, 2003; 14(10): 4207 - 4220. [Abstract] [Full Text] [PDF]
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S. Deaglio, A. Capobianco, L. Bergui, J. Durig, F. Morabito, U. Duhrsen, and F. Malavasi CD38 is a signaling molecule in B-cell chronic lymphocytic leukemia cells Blood, September 15, 2003; 102(6): 2146 - 2155. [Abstract] [Full Text] [PDF]
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K. G. Kohlgraf, A. J. Gawron, M. Higashi, J. L. Meza, M. D. Burdick, S. Kitajima, D. L. Kelly, T. C. Caffrey, and M. A. Hollingsworth Contribution of the MUC1 Tandem Repeat and Cytoplasmic Tail to Invasive and Metastatic Properties of a Pancreatic Cancer Cell Line Cancer Res., August 15, 2003; 63(16): 5011 - 5020. [Abstract] [Full Text] [PDF]
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X. A. Zhang, B. He, B. Zhou, and L. Liu Requirement of the p130CAS-Crk Coupling for Metastasis Suppressor KAI1/CD82-mediated Inhibition of Cell Migration J. Biol. Chem., July 11, 2003; 278(29): 27319 - 27328. [Abstract] [Full Text] [PDF]
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S. Martinez-Arca, V. Proux-Gillardeaux, P. Alberts, D. Louvard, and T. Galli Ectopic expression of syntaxin 1 in the ER redirects TI-VAMP- and cellubrevin-containing vesicles J. Cell Sci., July 1, 2003; 116(13): 2805 - 2816. [Abstract] [Full Text] [PDF]
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J. Lammerding, A. R. Kazarov, H. Huang, R. T. Lee, and M. E. Hemler Tetraspanin CD151 regulates {alpha}6{beta}1 integrin adhesion strengthening PNAS, June 24, 2003; 100(13): 7616 - 7621. [Abstract] [Full Text] [PDF]
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 S. Bauersachs, H. Blum, S. Mallok, H. Wenigerkind, S. Rief, K. Prelle, and E. Wolf Regulation of Ipsilateral and Contralateral Bovine Oviduct Epithelial Cell Function in the Postovulation Period: A Transcriptomics Approach Biol Reprod, April 1, 2003; 68(4): 1170 - 1177. [Abstract] [Full Text] [PDF]
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M. D. Gutierrez-Lopez, S. Ovalle, M. Yanez-Mo, N. Sanchez-Sanchez, E. Rubinstein, N. Olmo, M. A. Lizarbe, F. Sanchez-Madrid, and C. Cabanas A Functionally Relevant Conformational Epitope on the CD9 Tetraspanin Depends on the Association with Activated beta 1 Integrin J. Biol. Chem., January 3, 2003; 278(1): 208 - 218. [Abstract] [Full Text] [PDF]
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C. McCaig, C. M. Perks, and J. M. P. Holly Intrinsic actions of IGFBP-3 and IGFBP-5 on Hs578T breast cancer epithelial cells: inhibition or accentuation of attachment and survival is dependent upon the presence of fibronectin J. Cell Sci., November 15, 2002; 115(22): 4293 - 4303. [Abstract] [Full Text] [PDF]
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T. Uinuk-ool, W. E. Mayer, A. Sato, R. Dongak, M. D. Cooper, and J. Klein Lamprey lymphocyte-like cells express homologs of genes involved in immunologically relevant activities of mammalian lymphocytes PNAS, October 29, 2002; 99(22): 14356 - 14361. [Abstract] [Full Text] [PDF]
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L. G. Fradkin, J. T. Kamphorst, A. DiAntonio, C. S. Goodman, and J. N. Noordermeer Genomewide analysis of the Drosophila tetraspanins reveals a subset with similar function in the formation of the embryonic synapse PNAS, October 15, 2002; 99(21): 13663 - 13668. [Abstract] [Full Text] [PDF]
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A. R. Kazarov, X. Yang, C. S. Stipp, B. Sehgal, and M. E. Hemler An extracellular site on tetraspanin CD151 determines {alpha}3 and {alpha}6 integrin-dependent cellular morphology J. Cell Biol., September 29, 2002; 158(7): 1299 - 1309. [Abstract] [Full Text] [PDF]
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Y. Kawakami, K. Kawakami, W. F. A. Steelant, M. Ono, R. C. Baek, K. Handa, D. A. Withers, and S. Hakomori Tetraspanin CD9 Is a "Proteolipid," and Its Interaction with alpha 3 Integrin in Microdomain Is Promoted by GM3 Ganglioside, Leading to Inhibition of Laminin-5-dependent Cell Motility J. Biol. Chem., September 6, 2002; 277(37): 34349 - 34358. [Abstract] [Full Text] [PDF]
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L. Moro, L. Dolce, S. Cabodi, E. Bergatto, E. B. Erba, M. Smeriglio, E. Turco, S. F. Retta, M. G. Giuffrida, M. Venturino, et al. Integrin-induced Epidermal Growth Factor (EGF) Receptor Activation Requires c-Src and p130Cas and Leads to Phosphorylation of Specific EGF Receptor Tyrosines J. Biol. Chem., March 8, 2002; 277(11): 9405 - 9414. [Abstract] [Full Text] [PDF]
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