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Journal Articles
Transmembrane domain of CD44 is required for its detergent insolubility in fibroblasts
A. Perschl, J. Lesley, N. English, R. Hyman, I.S. Trowbridge
Journal of Cell Science 1995 108: 1033-1041;
A. Perschl
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J. Lesley
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N. English
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R. Hyman
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I.S. Trowbridge
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Summary

The hyaluronan receptor CD44 is an abundant glycoprotein expressed on a variety of different cell types. In fibroblasts a significant portion of receptor molecules remain in the detergent-insoluble fraction after Triton X-100 extraction. Detergent insolubility of these CD44 molecules has been interpreted to reflect their association with the cytoskeleton. In this study we examined the structural features of CD44 required for its Triton X-100 insolubility in murine fibroblasts. We expressed in L cells the wild-type hematopoietic form of CD44, a mutant CD44 lacking the cytoplasmic domain, and two mutant CD44 molecules with substituted transmembrane domains. Immunofluorescence and cell surface iodination were performed and the detergent extraction profile of the transfected CD44 molecules was determined. No difference in detergent solubility was observed between wild-type and tailless mutant-transfected molecules. However, both CD44 mutants with a heterologous transmembrane domain, derived from either the CD3 zeta chain or CD45, were completely soluble in Triton X-100. These results demonstrate that the transmembrane region but not the cytoplasmic domain of CD44 is required for the detergent-insolubility in these cells. No obvious colocalization of CD44 and actin stress fibers was observed before or after treatment with cytochalasin D, and no change in the detergent extraction profile of wild-type and mutant CD44 molecules was effected by cytochalasin D. In equilibrium density sucrose gradients the Triton-insoluble CD44 component was found in the low density fractions, indicating an association with Triton X-100-insoluble lipids.(ABSTRACT TRUNCATED AT 250 WORDS)

  • © 1995 by Company of Biologists

REFERENCES

    1. Aruffo A.,
    2. Stamenkovic I.,
    3. Melnick M.,
    4. Underhill C. B. and
    5. Seed B.
    (1990). CD44 is the principal cell surface receptor for hyaluronate. Cell 61, 1303–1313
    OpenUrlCrossRefPubMedWeb of Science
    1. Bertagnolli M. E. and
    2. Beckerle M. C.
    (1993). Evidence for the selective association of a subpopulation of GPIIb-IIIa with the actin cytoskeletons of thrombin-activated platelets. J. Cell Biol 121, 1329–1342
    OpenUrlAbstract/FREE Full Text
    1. Bourguignon L. Y. W.,
    2. Kalomiris E. L. and
    3. Lokeshwar V. B.
    (1991). Acylation of the lymphoma transmembrane glycoprotein, GP85 may be required for GP85-ankyrin interaction. J. Biol. Chem 266, 11761–11765
    OpenUrlAbstract/FREE Full Text
    1. Bourguignon L. Y. W.,
    2. Lokeshwar V. B.,
    3. He J.,
    4. Chen X. and
    5. Bourguignon G. J.
    (1992). A CD44-like endothelial cell transmembrane glycoprotein (GP116) interacts with extracellular matrix and ankyrin. Mol. Cell. Biol 12, 4464–4471
    OpenUrlAbstract/FREE Full Text
    1. Bourguignon L. Y. W.,
    2. Lokeshwar V. B.,
    3. Chen X. and
    4. Kerrick G. L.
    (1993). Hyaluronic acid-induced lymphocyte signal transduction and HA receptor (GP85/CD44)-cytoskeleton interaction. J. Immunol 151, 6634–6644
    OpenUrlAbstract
    1. Brown D. A. and
    2. Rose J. K.
    (1992). Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533–544
    OpenUrlCrossRefPubMedWeb of Science
    1. Brown S. S.,
    2. Malinoff H.L. and
    3. Wicha M. S.
    (1983). Connectin: Cell surface protein that binds both laminin and actin. Proc. Nat. Acad. Sci. USA 80, 5927–5930
    OpenUrlAbstract/FREE Full Text
    1. Brown T. A.,
    2. Bouchard T.,
    3. St. John T.,
    4. Wayner E. and
    5. Carter W. G.
    (1991). Human keratinocytes express a new CD44 core protein (CD44E) as a heparan-sulfate intrinsic membrane proteoglycan with additional exons. J. Cell Biol 113, 207–221
    OpenUrlAbstract/FREE Full Text
    1. Camp R. L.,
    2. Kraus T. A. and
    3. Pure E.
    (1991). Variations in the cytoskeletalinteraction and posttranslational modification of the CD44 homing receptor in macrophages. J. Cell Biol 115, 1283–1292
    OpenUrlAbstract/FREE Full Text
    1. Carpen O.,
    2. Pallai P.,
    3. Staunton D. E. and
    4. Springer T. A.
    (1992). Association of intercellular adhesion molecule-1 (ICAM-1) with actin-containing cytoskeleton and-actinin. J. Cell Biol 118, 1223–1234
    OpenUrlAbstract/FREE Full Text
    1. Carter W. G. and
    2. Wayner E. A.
    (1988). Characterization of the class III collagen receptor, a phosphorylated, transmembrane glycoprotein expressed in nucleated human cells. J. Biol. Chem 263, 4193–4201
    OpenUrlAbstract/FREE Full Text
    1. Cooper J. A.
    (1987). Effects of cytochalasin and phalloidin on actin. J. Cell Biol 105, 1473–1478
    OpenUrlFREE Full Text
    1. Dougherty G. J.,
    2. Landsorp P. M.,
    3. Cooper D. L. and
    4. Humphries R. K.
    (1991). Molecular cloning of CD44R1 and CD44R2, two novel isoforms of the human CD44 lymphocyte ‘homing’ receptor expressed by hemopoietic cells. J. Exp. Med 174, 1–5
    OpenUrlAbstract/FREE Full Text
    1. Gunthert U.,
    2. Hofmann M.,
    3. Rudy W.,
    4. Reber S.,
    5. Zoller M.,
    6. Haubmann I.,
    7. Matzku S.,
    8. Wenzel A.,
    9. Ponta H. and
    10. Herrlich P.
    (1991). A new variant of glycoprotein CD44 confers metastatic potential to rat carcinoma cells. Cell 65, 13–24
    OpenUrlCrossRefPubMedWeb of Science
    1. Hitchcock S.,
    2. Carlsson L. and
    3. Lindberg U.
    (1976). Depolymerization of F-actin by deoxyribonuclease I. Cell 7, 531–542
    OpenUrlCrossRefPubMedWeb of Science
    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. Hyman R.,
    2. Cunningham K. and
    3. Stallings V.
    (1980). Evidence for a genetic basis for the Class A Thy-1defect. Immunogenetics 10, 261–271
    OpenUrlCrossRefWeb of Science
    1. Hyman R.,
    2. Trowbridge I.,
    3. Stallings V. and
    4. Trotter J.
    (1982). Revertant expressing a structural variant of T200 glycoprotein. Immunogenetics 15, 413–420
    OpenUrlCrossRefPubMed
    1. Irving B. A. and
    2. Weiss A.
    (1991). The cytoplasmic domain of the T cell receptor zeta chain is sufficient to couple to receptor-associated signal transduction pathways. Cell 64, 891–901
    OpenUrlCrossRefPubMedWeb of Science
    1. Isacke C. M.
    (1994). The role of the cytoplasmic domain in regulating CD44 function. J. Cell Sci 107, 2353–2359
    OpenUrlFREE Full Text
    1. Jackson D. G.,
    2. Buckley J. and
    3. Bell J.
    (1992). Multiple variants of the human lymphocyte homing receptor CD44 generated by insertions at a single site in the extracellular domain. J. Biol. Chem 267, 4732–4739
    OpenUrlAbstract/FREE Full Text
    1. Jacobson K.,
    2. O'Dell D. and
    3. August J. T.
    (1984). Redistribution of a major cell surface glycoprotein during cell movement. J. Cell Biol 99, 1613–1623
    OpenUrlAbstract/FREE Full Text
    1. Jacobson K.,
    2. O'Dell D. and
    3. August J. T.
    (1984). Lateral diffusion of an 80,000-dalton glycoprotein in the plasma membrane of murine fibroblasts: Relationships to cell structure and function. J. Cell Biol 99, 1624–1633
    OpenUrlAbstract/FREE Full Text
    1. Knudson C. B. and
    2. Knudson W.
    (1993). Hyaluronan-binding proteins in development, tissue homeostasis, and disease. FASEB J 7, 1233–1241
    OpenUrlAbstract
    1. Kuhn L. C.,
    2. McClelland A. and
    3. Ruddle F. H.
    (1984). Gene transfer, expression and molecular cloning of the human transferrin receptor gene. Cell 37, 95–103
    OpenUrlCrossRefPubMedWeb of Science
    1. Kunkel T. A.
    (1985). Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Nat. Acad. Sci. USA 82, 488–492
    OpenUrlAbstract/FREE Full Text
    1. Lacy B. E. and
    2. Underhill C. B.
    (1987). The hyaluronate receptor is associated with actin filaments. J. Cell Biol 105, 1395–1404
    OpenUrlAbstract/FREE Full Text
    1. Laurent T. C. and
    2. Fraser J. R. E.
    (1992). Hyaluronan. FASEB J 6, 2397–2404
    OpenUrlAbstract
    1. Lesley J. and
    2. Trowbridge I. S.
    (1982). Genetic characterization of a murine polymorphic cell surface glycoprotein. Immunogenetics 15, 313–320
    OpenUrlCrossRefPubMedWeb of Science
    1. Lesley J.,
    2. He Q.,
    3. Miyake K.,
    4. Hamann A.,
    5. Hyman R. and
    6. Kincade P. W.
    (1992). Requirements for hyaluronic acid binding by CD44: a role for the cytoplasmic domain and activation by antibody. J. Exp. Med 175, 257–266
    OpenUrlAbstract/FREE Full Text
    1. Lisanti M. P.,
    2. Scherer P. E.,
    3. Vidurgieriene J.,
    4. Tang Z. L.,
    5. Hermanowshi-Vosatka A.,
    6. Tu Y.-H.,
    7. Cook R. F. and
    8. Sargiacomo M.
    (1994). Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: Implications for human disease. J. Cell Biol 226, 111–126
    OpenUrl
    1. Lokeshar V. B.,
    2. Fregien N. and
    3. Bourguignon L. Y. W.
    (1994). Ankyrin-binding domain of CD44 (GP85). is required for the expression of hyaluronic-acid-mediated adhesion function. J. Cell Biol 126, 1099–1109
    OpenUrlAbstract/FREE Full Text
    1. Luna E. J. and
    2. Hitt A. L.
    (1992). Cytoskeleton-plasma membrane interactions. Science 258, 955–964
    OpenUrlAbstract/FREE Full Text
    1. Miettinen H. M. and
    2. Jalkanen M.
    (1994). The cytoplasmic domain of syndecan-1 is not required for association with Triton-X-100-insoluble material. J. Cell Sci 107, 1571–1581
    OpenUrlAbstract/FREE Full Text
    1. Morris A. and
    2. Tannenbaum J.
    (1980). Cytochalasin D does not produce net depolymerization of actin filaments in HEp-2 cells. Nature 287, 637–639
    OpenUrlCrossRefPubMed
    1. Neame S. J. and
    2. Isacke C. M.
    (1992). Phosphorylation of CD44 in vivo requires both ser323 and ser325, but does not regulate membrane localization or cytoskeletal interaction in epithelial cells. EMBO J 11, 4733–4738
    OpenUrlPubMed
    1. Neame S. J. and
    2. Isacke C. M.
    (1993). The cytoplasmic tail of CD44 is required for basolateral localization in epithelial MDCK cells but does not mediate association with the detergent-insoluble cytoskeleton in fibroblasts. J. Cell Biol 121, 1299–1310
    OpenUrlAbstract/FREE Full Text
    1. Nottenburg C.,
    2. Rees G. and
    3. St. John J.
    (1989). Isolation of mouse CD44 cDNA: Structural features are distinct from the primate cDNA. Proc. Nat. Acad. Sci. USA 86, 8521–8525
    OpenUrlAbstract/FREE Full Text
    1. Otey C. A.,
    2. Pavalko F. M. and
    3. Burridge K.
    (1990). An interaction between-actinin and the 1integrin subunit in vitro. J. Cell Biol 111, 721–729
    OpenUrlAbstract/FREE Full Text
    1. Rodgers W.,
    2. Crise B. and
    3. Rose J. K.
    (1994). Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction. Mol. Cell. Biol 14, 5384–5391
    OpenUrlAbstract/FREE Full Text
    1. Romeo C. and
    2. Seed B.
    (1991). Cellular immunity to HIV activated by CD4 fused to T cell or Fc receptor polypeptides. Cell 64, 1037–1046
    OpenUrlCrossRefPubMedWeb of Science
    1. Skibbens J. E.,
    2. Roth M. G. and
    3. Matlin K. S.
    (1989). Differential extractibility of influenza virus hemaglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts. J. Cell Biol 108, 821–823
    OpenUrlAbstract/FREE Full Text
    1. Stamenkovic I.,
    2. Amiot M.,
    3. Pesandro J. M. and
    4. Seed B.
    (1989). A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family. Cell 56, 1057–1062
    OpenUrlCrossRefPubMedWeb of Science
    1. Tarone G.,
    2. Ferracini R.,
    3. Galetto G. and
    4. Comoglio P.
    (1984). A cell surface integral membrane glycoprotein of 85,000 mol wt (gp85) associated with Triton X-100 insoluble cell skeleton. J. Cell Biol 99, 512–519
    OpenUrlAbstract/FREE Full Text
    1. Thomas L.,
    2. Byers H. R.,
    3. Vink J. and
    4. Stamenkovic I.
    (1992). CD44H regulates tumor cell migration on hyaluronate-coated substrate. J. Cell Biol 118, 971–977
    OpenUrlAbstract/FREE Full Text
    1. Todaro G. and
    2. Green H.
    (1963). Quantitative studies of the growth of mouse embryo cells in culture and their development into established cell lines. J. Cell Biol 17, 299–313
    OpenUrlAbstract/FREE Full Text
    1. Trowbridge I. S.,
    2. Lesley J.,
    3. Schulte R.,
    4. Hyman R. and
    5. Trotter J.
    (1982). Biochemical characterization and cellular distribution of a polymorphic, murine cell-surface glycoprotein expressed on lymphoid tissues. Immunogenetics 15, 299–312
    OpenUrlCrossRefPubMedWeb of Science
    1. Tsukita S.,
    2. Oishi K.,
    3. Sato N.,
    4. Sagara J.,
    5. Kawai A. and
    6. Tsukita S.
    (1994). ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeleton. J. Cell Biol 126, 391–401
    OpenUrlAbstract/FREE Full Text
    1. Weissman A. M.,
    2. Baniyash M.,
    3. Hou D.,
    4. Samelson L. E.,
    5. Burgess W. H. and
    6. Klausner R. D.
    (1988). Molecular cloning of the zeta chain of the T cell antigen receptor. Science 239, 1018–1021
    OpenUrlAbstract/FREE Full Text
    1. Yahara I.,
    2. Harada F.,
    3. Sekita S.,
    4. Yoshihira K. and
    5. Natori S.
    (1982). Correlation between effects of 24 different cytochalasins on cellular structures and cellular events and those on actin in vitro. J. Cell Biol 92, 69–78
    OpenUrlAbstract/FREE Full Text
    1. Yu J.,
    2. Fishman D. and
    3. Steck T.
    (1973). Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergents. J. Supramol. Struct 1, 233–248
    OpenUrlCrossRefPubMed
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Journal Articles
Transmembrane domain of CD44 is required for its detergent insolubility in fibroblasts
A. Perschl, J. Lesley, N. English, R. Hyman, I.S. Trowbridge
Journal of Cell Science 1995 108: 1033-1041;
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Transmembrane domain of CD44 is required for its detergent insolubility in fibroblasts
A. Perschl, J. Lesley, N. English, R. Hyman, I.S. Trowbridge
Journal of Cell Science 1995 108: 1033-1041;

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