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alpha 3A beta 1 integrin localizes to focal contacts in response to diverse extracellular matrix proteins
C.M. DiPersio, S. Shah, R.O. Hynes
Journal of Cell Science 1995 108: 2321-2336;

Summary

In vitro binding assays and inhibition of cell adhesion with monoclonal antibodies have implicated the integrin alpha 3 beta 1 as a receptor for a variety of extracellular ligands. However, reports of alpha 3 beta 1-ligand interactions are inconsistent, and transfection studies have suggested that alpha 3 beta 1 is not sufficient for cell attachment to ligands other than kalinin/laminin 5. We used immunofluorescence to study subcellular localization of the alpha 3A cytoplasmic domain variant in different cultured cell types. Using standard fixation and permeabilization methods, antibodies specific for alpha 3A stained most cell types in a diffuse pattern, consistent with previous reports. Surprisingly, however, chemical cross-linking of integrins to the extracellular matrix and extraction of the cytoskeleton prior to immunofluorescence revealed alpha 3A in focal contacts of most cells tested, suggesting that the cytoplasmic domain was concealed in intact focal contacts by cytoskeletal or other cytoplasmic proteins. The alpha 3A subunit localized to focal contacts in several cell types cultured on fibronectin, kalinin/laminin 5, EHS-laminin/laminin 1, type IV collagen, or vitronectin. In contrast, alpha 5 and alpha V integrins were detected in focal contacts only in cells grown on their known ligands (fibronectin, and fibronectin or vitronectin, respectively). Therefore, our results show that alpha 3A beta 1 responds to a broad spectrum of extracellular ligands. Time course comparisons of the recruitment of alpha subunits from different fibronectin receptors suggested that localization of alpha 3A beta 1 to fibronectin-induced focal contacts was independent of the recruitment of alpha 5 and alpha 4 integrins. However, other studies have shown that alpha 3A beta 1 does not mediate initial cell adhesion to many of the ligands that induced its focal contact localization, including fibronectin. Therefore, we suggest that alpha 3A beta 1 may be a secondary receptor with post-cell-adhesion functions for a broad spectrum of extracellular matrices.

REFERENCES

    1. Adams J. C. and
    2. Watt F. M.
    (1991). Expression of1, 3,4, and 5 integrins by human epidermal keratinocytes and non-differentiating keratinocytes. J. Cell Biol 115, 829–841
    OpenUrlAbstract/FREE Full Text
    1. Adler S.
    (1992). Integrin receptors in the glomerulus: potential role in glomerular injury. Am. J. Physiol 262, 696–.
    OpenUrl
    1. Bartolazzi A.,
    2. Cerboni C.,
    3. Nicotra M. R.,
    4. Mottolese M.,
    5. Bigotti A. and
    6. Natali P. G.
    (1994). Transformation and tumor progression are frequently associated with expression of the3/ 1 heterodimer in solid tumors. Int. J. Cancer 58, 488–491
    OpenUrlPubMed
    1. Briesewitz R.,
    2. Kern A. and
    3. Marcantonio E. E.
    (1993). Ligand-dependent and-independent integrin focal contact localization: the role of thechain cytoplasmic domain. Mol. Cell Biol 4, 593–604
    OpenUrl
    1. Burridge K.,
    2. Fath K.,
    3. Kelly T.,
    4. Nuckolls G. and
    5. Turner C.
    (1988). Focaladhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol 4, 487–525
    OpenUrlCrossRefWeb of Science
    1. Busk M.,
    2. Pytela R. and
    3. Sheppard D.
    (1992). Characterization of the integrinV 6 as a fibronectin-binding protein. J. Biol. Chem 267, 5790–5796
    OpenUrlAbstract/FREE Full Text
    1. Carter W. G.,
    2. Wayner E. A.,
    3. Bouchard T. S. and
    4. Kaur P.
    (1990). The role of integrins2 1 and3 1 in cell-cell and cell-substrate adhesion of human epidermal cells. J. Cell Biol 110, 1387–1404
    OpenUrlAbstract/FREE Full Text
    1. Carter W. G.,
    2. Kaur P.,
    3. Gil S. G.,
    4. Gahr P. J. and
    5. Wayner E. A.
    (1990). Distinct functions for integrins3 1 in focal adhesions and6 4/bullous antigen in a new stable anchoring contact (SAC) of keratinocytes: relation to hemidesmosomes. J. Cell Biol 111, 3141–3154
    OpenUrlAbstract/FREE Full Text
    1. Carter W. G.,
    2. Ryan M. C. and
    3. Gahr P. J.
    (1991). Epiligrin, a new cell adhesion ligand for integrin3 1 in epithelial basement membranes. Cell 65, 599–610
    OpenUrlCrossRefPubMedWeb of Science
    1. Chan B. M. C.,
    2. Elices M. J.,
    3. Murphy E. and
    4. Hemler M. E.
    (1992). Adhesion to vascular cell adhesion molecule 1 and fibronectin: comparison of4 1 (VLA-4) and4 7 on the human B cell line JY. J. Biol. Chem 267, 8366–8370
    OpenUrlAbstract/FREE Full Text
    1. Chan B. M. C.,
    2. Kassner P. D.,
    3. Schiro J. A.,
    4. Byers H. R.,
    5. Kupper T. S. and
    6. Hemler M. E.
    (1992). Distinct cellular functions mediated by different VLA integrinsubunit cytoplasmic domains. Cell 68, 1051–1060
    OpenUrlCrossRefPubMedWeb of Science
    1. Charo I. F.,
    2. Nannizzi L.,
    3. Smith J. W. and
    4. Cheresh D. A.
    (1990). The vitronectin receptorV 3 binds fibronectin and acts in concert with5 1 in promoting cellular attachment and spreading on fibronectin. J. Cell Biol 111, 2795–2800
    OpenUrlAbstract/FREE Full Text
    1. Chen C. S.,
    2. Thiagarajan P.,
    3. Schwartz S. M.,
    4. Harlan J. M. and
    5. Heimark R. L.
    (1987). The platelet glycoprotein IIb/IIIa-like protein in human endothelial cells promotes adhesion but not initial attachment to extracellular matrix. J. Cell Biol 105, 1885–1892
    OpenUrlAbstract/FREE Full Text
    1. Cheresh D. A.
    (1987). Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor. Proc. Nat. Acad. Sci. USA 84, 6471–6475
    OpenUrlAbstract/FREE Full Text
    1. Clyman R. I.,
    2. Mauray F. and
    3. Kramer R. H.
    (1992). 1 and 3 integrins have different roles in the adhesion and migration of vascular smooth muscle cells on extracellular matrix. Exp. Cell Res 200, 272–284
    OpenUrlCrossRefPubMedWeb of Science
    1. Dedhar S. and
    2. Saulnier R.
    (1990). Alterations in integrin receptor expression on chemically transformed human cells: specific enhancement of laminin and collagen receptors. J. Cell Biol 110, 481–489
    OpenUrlAbstract/FREE Full Text
    1. Dedhar S.,
    2. Jewell K.,
    3. Rojiani M. and
    4. Gray V.
    (1992). The receptor for the basement membrane glycoprotein entactin is the integrin3 1. J. Biol. Chem 267, 18908–18914
    OpenUrlAbstract/FREE Full Text
    1. Delwel G. O.,
    2. de Melker A. A.,
    3. Hogervorst F.,
    4. Jaspars L. H.,
    5. Fles D. L. A.,
    6. Kuikman I.,
    7. Lindblom A.,
    8. Paulsson M.,
    9. Timpl R. and
    10. Sonnenberg A.
    (1994). Distinct and overlapping ligand specificities of the3A 1 and6A 1 integrins: recognition of laminin isoforms. Mol. Biol. Cell 5, 203–215
    OpenUrlAbstract/FREE Full Text
    1. Elices M. J. and
    2. Hemler M. E.
    (1989). The human integrin VLA-2 is a collagen receptor on some cells and a collagen/laminin receptor on others. Proc. Nat. Acad. Sci. USA 86, 9906–9910
    OpenUrlAbstract/FREE Full Text
    1. Elices M. J.,
    2. Osborn L.,
    3. Takada Y.,
    4. Crouse C.,
    5. Luhowskyj S.,
    6. Hemler M. E. and
    7. Lobb R. R.
    (1990). VCAM-1 on activated endothelium interacts with the leukocyte integrin VLA-4 at a site distinct from the VLA-4/fibronectin binding site. Cell 60, 577–584
    OpenUrlCrossRefPubMedWeb of Science
    1. Elices M. J.,
    2. Urry L. A. and
    3. Hemler M. E.
    (1991). Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by ARG-GLY-ASP peptide and by divalent cations. J. Cell Biol 112, 169–181
    OpenUrlAbstract/FREE Full Text
    1. Enomoto M. I.,
    2. Boettiger D. and
    3. Menko A. S.
    (1993). 5 Integrin is a critical component of adhesion plaques in myogenesis. Dev. Biol 155, 180–197
    OpenUrlCrossRefPubMedWeb of Science
    1. Enomoto-Iwamoto M.,
    2. Menko A. S.,
    3. Philp N. and
    4. Boettiger D.
    (1993). Evaluation of integrin molecules involved in substrate adhesion. Cell Adhes. Commun 1, 191–202
    OpenUrlPubMed
    1. Fradet Y.,
    2. Cordon-Cardo C.,
    3. Thomson T.,
    4. Daly M. E.,
    5. Whitmore W. F. Jr..,
    6. Lloyd K. O.,
    7. Melamed M. R. and
    8. Old L. J.
    (1984). Cell surface antigens of human bladder cancer defined by mouse monoclonal antibodies. Proc. Nat. Acad. Sci. USA 81, 224–228
    OpenUrlAbstract/FREE Full Text
    1. Gehlsen K. R.,
    2. Dillner L.,
    3. Engvall E. and
    4. Ruoslahti E.
    (1988). The human laminin receptor is a member of the integrin family of cell adhesion receptors. Science 241, 1228–1229
    OpenUrlAbstract/FREE Full Text
    1. Gehlsen K. R.,
    2. Dickerson K.,
    3. Argraves W. S.,
    4. Engvall E. and
    5. Ruoslahti E.
    (1989). Subunit structure of a laminin-binding integrin and localization of its binding site on laminin. J. Biol. Chem 264, 19034–19038
    OpenUrlAbstract/FREE Full Text
    1. Grenz H.,
    2. Carbonetto S. and
    3. Goodman S. L.
    (1993). 3 1 Integrin is moved into focal contacts in kidney mesangial cells. J. Cell Sci 105, 739–751
    OpenUrlAbstract/FREE Full Text
    1. Guan J.-L. and
    2. Hynes R. O.
    (1990). Lymphoid cells recognize an alternatively spliced segment of fibronectin via the integrin receptor4 1. Cell 60, 53–61
    OpenUrlCrossRefPubMedWeb of Science
    1. Guan J.-L.,
    2. Trevithick J. E. and
    3. Hynes R. O.
    (1991). Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120 kDa protein. Cell Regul 2, 951–964
    OpenUrlPubMedWeb of Science
    1. Hemler M. E.,
    2. Huang C. and
    3. Schwarz L.
    (1987). The VLA protein family. J. Biol. Chem 262, 3300–3309
    OpenUrlAbstract/FREE Full Text
    1. Horwitz A.,
    2. Duggan K.,
    3. Buck C.,
    4. Beckerle M. C. and
    5. Burridge K.
    (1986). Interaction of plasma membrane fibronectin receptor with talin-a transmembrane linkage. Nature 320, 531–533
    OpenUrlCrossRefPubMed
    1. Hynes R. O.,
    2. Marcantonio E. E.,
    3. Stepp M. A.,
    4. Urry L. A. and
    5. Yee G. H.
    (1989). Integrin heterodimer and receptor complexity in avian and mammalian cells. J. Cell Biol 109, 409–420
    OpenUrlAbstract/FREE Full Text
    1. Hynes R. O.
    (1992). Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11–25
    OpenUrlCrossRefPubMedWeb of Science
    1. Juliano R. L. and
    2. Haskill S.
    (1993). Signal transduction from the extracellular matrix. J. Cell Biol 120, 577–585
    OpenUrlFREE Full Text
    1. Kawaguchi S.,
    2. Bergelson J. M.,
    3. Finberg R. W. and
    4. Hemler M. E.
    (1994). Integrin2 cytoplasmic domain deletion effects: loss of adhesive activity parallels ligand-independent recruitment into focal adhesions. Mol. Biol. Cell 5, 977–988
    OpenUrlAbstract/FREE Full Text
    1. Kirchhofer D.,
    2. Languino L. R.,
    3. Ruoslahti E. and
    4. Pierschbacher M. D.
    (1990). 2 1 integrins from different cell types show different binding specificities. J. Biol. Chem 265, 615–618
    OpenUrlAbstract/FREE Full Text
    1. Kornberg L. J.,
    2. Earp H. S.,
    3. Turner C. E.,
    4. Prockop C. and
    5. Juliano R. L.
    (1991). Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of1 integrins. Proc. Nat. Acad. Sci. USA 88, 8392–8396
    OpenUrlAbstract/FREE Full Text
    1. LaFlamme S. E.,
    2. Akiyama S. K. and
    3. Yamada K. M.
    (1992). Regulation of fibronectin receptor distribution. J. Cell Biol 117, 437–447
    OpenUrlAbstract/FREE Full Text
    1. Marcantonio E. E. and
    2. Hynes R. O.
    (1988). Antibodies to the conserved cytoplasmic domain of the integrin1 cytoplasmic domain by site directed mutagenesis. J. Cell Biol 106, 1765–1772
    OpenUrlAbstract/FREE Full Text
    1. Mayadas T. N.,
    2. Johnson R. C.,
    3. Rayburn H.,
    4. Hynes R. O. and
    5. Wagner D. D.
    (1993). Leukocyte rolling and extravasation are severely compromised in P-selectin-deficient mice. Cell 74, 541–544
    OpenUrlCrossRefPubMedWeb of Science
    1. Mould A. P.,
    2. Wheldon L. A.,
    3. Komoriya A.,
    4. Wayner E. A.,
    5. Yamada K. M. and
    6. Humphries M. J.
    (1990). Affinity chromatographic isolation of the melanoma adhesion receptor for the IIICS region of fibronectin and its identification as the integrin alpha 4 beta 1. J. Biol. Chem 265, 4020–4024
    OpenUrlAbstract/FREE Full Text
    1. Otey C. A.,
    2. Pavalko F. M. and
    3. Burridge K.
    (1990). An interaction between-actinin and the 1 integrin subunit in vitro. J. Cell Biol 111, 721–729
    OpenUrlAbstract/FREE Full Text
    1. Patey N.,
    2. Halbwachs-Mecarelli L.,
    3. Droz D.,
    4. Lesavre P. and
    5. Noel L. H.
    (1994). Distribution of integrin subunits in normal human kidney. Cell Adhes. Commun 2, 159–167
    OpenUrlPubMedWeb of Science
    1. Peltonen J.,
    2. Larjava H.,
    3. Jaakkola S.,
    4. Gralnick H.,
    5. Akiyama S. K.,
    6. Yamada S. S.,
    7. Yamada K. M. and
    8. Uitto J.
    (1989). Localization of integrin receptors for fibronectin, collagen, and laminin in human skin. J. Clin. Invest 84, 1916–1923
    OpenUrlPubMedWeb of Science
    1. Plantefaber L. C. and
    2. Hynes R. O.
    (1989). Changes in integrin receptors on oncogenically transformed cells. Cell 56, 281–290
    OpenUrlCrossRefPubMedWeb of Science
    1. Pytela R.,
    2. Pierschbacher M. D. and
    3. Ruoslahti E.
    (1985). Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor. Cell 40, 191–198
    OpenUrlCrossRefPubMedWeb of Science
    1. Rettig W. J.,
    2. Murty V. S.,
    3. Mattes M. J.,
    4. Chaganti R. S. K. and
    5. Old L. J.
    (1986). Extracellular matrix-modulated expression of human cell surface glycoproteins A42 and J143: Intrinsic and extrinsic signals determine antigenic phenotypes. J. Exp. Med 164, 1581–1599
    OpenUrlAbstract/FREE Full Text
    1. Rouselle P.,
    2. Lunstrum G. P.,
    3. Keene D. R. and
    4. Burgeson R. E.
    (1991). Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J. Cell Biol 114, 567–576
    OpenUrlAbstract/FREE Full Text
    1. Ruegg C.,
    2. Postigo A. A.,
    3. Sikorski E. E.,
    4. Butcher E. C.,
    5. Pytela R. and
    6. Erle D. J.
    (1992). Role of integrin4 7/4 P in lymphocyte adherence to fibronectin and VCAM-1 and in homotypic cell clustering. J. Cell Biol 117, 179–189
    OpenUrlAbstract/FREE Full Text
    1. Schaller M. D.,
    2. Borgman C. A.,
    3. Cobb B. S.,
    4. Vines R. R.,
    5. Reynolds A. B. and
    6. Parsons J. T.
    (1992). pp125 FAK, a structurally unique protein tyrosine kinase associated with focal adhesions. Proc. Nat. Acad. Sci. USA 89, 5192–5196
    OpenUrlAbstract/FREE Full Text
    1. Shaw L. M.,
    2. Lotz M. M. and
    3. Mercurio A. M.
    (1993). Inside-out integrin signaling in macrophages. J. Biol. Chem 268, 11401–11408
    OpenUrlAbstract/FREE Full Text
    1. Springer T. A.
    (1994). Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 76, 301–314
    OpenUrlCrossRefPubMedWeb of Science
    1. Sriramarao P.,
    2. Steffner P. and
    3. Gehlsen K. R.
    (1993). Biochemical evidence for a homophilic interaction of the3 1 integrin. J. Biol. Chem 268, 22036–22041
    OpenUrlAbstract/FREE Full Text
    1. Staatz W. D.,
    2. Rajpara S. M.,
    3. Wayner E. A.,
    4. Carter W. G. and
    5. Santoro S. A.
    (1989). The membrane glycoprotein Ia-IIa (VLA-2) complex mediates the Mg++-dependent adhesion of platelets to collagen. J. Cell Biol 108, 1987–1924
    OpenUrlAbstract/FREE Full Text
    1. Staquet M. J.,
    2. Levarlet B.,
    3. Dezutter-Dambuyant C.,
    4. Schmitt D. and
    5. Thivolet J.
    (1990). Identification of specific human epithelial cell integrin receptors as VLA proteins. Exp. Cell Res 187, 277–283
    OpenUrlCrossRefPubMedWeb of Science
    1. Symington B. E.,
    2. Takada Y. and
    3. Carter W. G.
    (1993). Interaction of integrins3 1 and2 1: potential role in keratinocyte intercellular adhesion. J. Cell Biol 120, 523–535
    OpenUrlAbstract/FREE Full Text
    1. Takada Y.,
    2. Murphy E.,
    3. Pil P.,
    4. Chen C.,
    5. Ginsberg M. H. and
    6. Hemler M. E.
    (1991). Molecular cloning and expression of the cDNA for3 subunit of human 31 (VLA-3), an integrin receptor for fibronectin, laminin, and collagen. J. Cell Biol 115, 257–266
    OpenUrlAbstract/FREE Full Text
    1. Takada Y.,
    2. Ylänne J.,
    3. Mandelman D.,
    4. Puzon W. and
    5. Ginsberg. M.
    (1992). A point mutation of integrin1 subunit blocks binding of 51 to fibronectin and invasin but not recruitment to adhesion plaques. J. Cell Biol 119, 913–921
    OpenUrlAbstract/FREE Full Text
    1. Tamura R. N.,
    2. Cooper H. M.,
    3. Collo G. and
    4. Quaranta V.
    (1991). Cell type-specific integrin variants with alternativechain cytoplasmic domains. Proc. Nat. Acad. Sci. USA 88, 10183–10187
    OpenUrlAbstract/FREE Full Text
    1. Tomaselli K. J.,
    2. Hall D. E.,
    3. Reichardt L. T.,
    4. Flier L. A.,
    5. Gehlsen K. R.,
    6. Turner D. C. and
    7. Carbonetto S.
    (1990). A neuronal cell line (PC12) expresses two1-class integrins- 11 and 31-that recognize different neurite outgrowth domains in laminin. Neuron 5, 651–662
    OpenUrlCrossRefPubMedWeb of Science
    1. Tsuji T.,
    2. Yamamoto F.-i.,
    3. Miura Y.,
    4. Takio K.,
    5. Titani K.,
    6. Pawar S.,
    7. Osawa T. and
    8. Hakomori S.-i
    (1990). Characterization through cDNA cloning of galactoprotein b3 (Gap b3), a cell surface membrane glycoprotein showing enhanced expression on oncogenic transformation. Identification ofGap b3 as a member of the integrin superfamily. J. Biol. Chem 265, 7016–7021
    OpenUrlAbstract/FREE Full Text
    1. Vogel B. E.,
    2. Tarone G.,
    3. Giancotti F. G.,
    4. Gailit J. and
    5. Ruoslahti E.
    (1990). A novel fibronectin receptor with an unexpected subunit composition (V 1). J. Biol. Chem 265, 5934–5937
    OpenUrlAbstract/FREE Full Text
    1. Wayner E. A. and
    2. Carter W. G.
    (1987). Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cells possessing uniqueand common subunits. J. Cell Biol 105, 1873–1884
    OpenUrlAbstract/FREE Full Text
    1. Wayner E. A.,
    2. Carter W. G.,
    3. Piotrowicz R. S. and
    4. Kunicki T. J.
    (1988). The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoproteins IIc-IIa. J. Cell Biol 107, 1881–1891
    OpenUrlAbstract/FREE Full Text
    1. Wayner E. A.,
    2. Garcia P. A.,
    3. Humphries M. J.,
    4. McDonald J. A. and
    5. Carter W. G.
    (1989). Identification and characterization of the T lymphocyte adhesion receptor for an alternative cell attachment domain (CS-1) in plasma fibronectin. J. Cell Biol 109, 1321–1330
    OpenUrlAbstract/FREE Full Text
    1. Wayner E. A.,
    2. Orlando R. A. and
    3. Cheresh D. A.
    (1991). IntegrinsV 3 andV 5 contribute to cell attachment to vitronectin but differentially distribute on the cell surface. J. Cell Biol 113, 919–929
    OpenUrlAbstract/FREE Full Text
    1. Wayner E. A.,
    2. Gil S. G.,
    3. Murphy G. F.,
    4. Wilke M. S. and
    5. Carter W. G.
    (1993). Epiligrin, a component of epithelial basement membranes, is an adhesive ligand for3 1 positive T lymphocytes. J. Cell Biol 121, 1141–1152
    OpenUrlAbstract/FREE Full Text
    1. Weitzman J. B.,
    2. Pasqualini R.,
    3. Takada Y. and
    4. Hemler M. E.
    (1993). The function and distinctive regulation of the integrin VLA-3 in cell adhesion, spreading, and homotypic cell aggregation. J. Biol. Chem 268, 8651–8657
    OpenUrlAbstract/FREE Full Text
    1. Ylänne J.,
    2. Chen Y.,
    3. O'Toole T. E.,
    4. Loftus J. C.,
    5. Takada Y. and
    6. Ginsberg M. H.
    (1993). Distinct functions of integrinand subunit cytoplasmic domains in cell spreading and formation of focal adhesions. J. Cell Biol 122, 223–233
    OpenUrlAbstract/FREE Full Text
    1. Zachary I. and
    2. Rozengurt E.
    (1992). Focal adhesion kinase (p125FAK): a point of convergence in the action of neuropeptides, integrins, and oncogenes. Cell 71, 891–894
    OpenUrlCrossRefPubMedWeb of Science
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Journal Articles
alpha 3A beta 1 integrin localizes to focal contacts in response to diverse extracellular matrix proteins
C.M. DiPersio, S. Shah, R.O. Hynes
Journal of Cell Science 1995 108: 2321-2336;
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