메뉴 건너뛰기




Volumn 146, Issue 4, 1999, Pages 843-854

Analysis of CD44-containing lipid rafts: Recruitment of annexin II and stabilization by the actin cytoskeleton

Author keywords

Annexin II; CD44; Cytoskeleton; Epithelial cell line; Lipid rafts

Indexed keywords

CHOLESTEROL; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); HERMES ANTIGEN; LIPOCORTIN 2; PHALLOIDIN;

EID: 0033598190     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.146.4.843     Document Type: Article
Times cited : (366)

References (70)
  • 2
    • 0031847686 scopus 로고    scopus 로고
    • Localization of autocrine motility factor receptor to caveolae and clathrin-independent internalization of its ligand to smooth endoplasmic reticulum
    • Benlimame, N., P.U. Le, and I.R. Nabi. 1998. Localization of autocrine motility factor receptor to caveolae and clathrin-independent internalization of its ligand to smooth endoplasmic reticulum. Mol. Biol. Cell. 9:1773-1786.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 1773-1786
    • Benlimame, N.1    Le, P.U.2    Nabi, I.R.3
  • 3
    • 0001518680 scopus 로고    scopus 로고
    • CD44 isoform-cytoskeleton interaction in oncogenic signaling and tumor progression
    • Bourguignon, L., D. Zhu, and H. Zhu. 1998. CD44 isoform-cytoskeleton interaction in oncogenic signaling and tumor progression. Front. Biosci. 3:637-649.
    • (1998) Front. Biosci. , vol.3 , pp. 637-649
    • Bourguignon, L.1    Zhu, D.2    Zhu, H.3
  • 4
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: What physical studies of model membranes reveal
    • Brown, R. 1998. Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J. Cell Sci. 111:1-9.
    • (1998) J. Cell Sci. , vol.111 , pp. 1-9
    • Brown, R.1
  • 5
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D.A., and E. London. 1998. Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14:111-136.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 6
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphale 5-kinase in mammalian cells
    • Chong, L.D., A. Traynor-Kaplan, G.M. Bokoch, and M.A. Schwartz. 1994. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphale 5-kinase in mammalian cells. Cell. 79:507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 7
    • 0026452240 scopus 로고
    • The annexins and exocytosis
    • Creutz, C.E. 1992. The annexins and exocytosis. Science. 258:924-931.
    • (1992) Science , vol.258 , pp. 924-931
    • Creutz, C.E.1
  • 8
    • 0018096805 scopus 로고
    • Freeze-fracture identification of sterol-digitonin complexes in cell and liposome membranes
    • Elias, P.M., J. Goerke, D.S. Friend, and B.E. Brown. 1978. Freeze-fracture identification of sterol-digitonin complexes in cell and liposome membranes. J. Cell Biol. 78:577-596.
    • (1978) J. Cell Biol. , vol.78 , pp. 577-596
    • Elias, P.M.1    Goerke, J.2    Friend, D.S.3    Brown, B.E.4
  • 10
    • 0029670092 scopus 로고    scopus 로고
    • The estrogen-dependent c-JunER protein causes a reversible loss of mammary epithelial cell polarity involving a destabilisation of adherens junctions
    • Fialka, I., H. Schwarz, E. Reichmann, M. Oft, M. Busslinger, and H. Beug. 1996. The estrogen-dependent c-JunER protein causes a reversible loss of mammary epithelial cell polarity involving a destabilisation of adherens junctions. J. Cell Biol. 132:1115-1132.
    • (1996) J. Cell Biol. , vol.132 , pp. 1115-1132
    • Fialka, I.1    Schwarz, H.2    Reichmann, E.3    Oft, M.4    Busslinger, M.5    Beug, H.6
  • 11
    • 0010614589 scopus 로고    scopus 로고
    • Three-dimensional organotypic growth of epithelial cells in reconstituted extracellular matrix
    • J.E. Celis, editor. Academic Press, San Diego, CA
    • Fialka, I., M. Oft, E. Reichmann, L.A. Huber, and H. Beug. 1997. Three-dimensional organotypic growth of epithelial cells in reconstituted extracellular matrix. In Cell Biology: A Laboratory Handbook. 2nd edition. J.E. Celis, editor. Academic Press, San Diego, CA. 1:107-112.
    • (1997) Cell Biology: a Laboratory Handbook. 2nd Edition , vol.1 , pp. 107-112
    • Fialka, I.1    Oft, M.2    Reichmann, E.3    Huber, L.A.4    Beug, H.5
  • 12
    • 0030809601 scopus 로고    scopus 로고
    • Intracellular cholesterol transport
    • Fielding, C.J., and P.E. Fielding. 1997. Intracellular cholesterol transport. J. Lipid Res. 38:1503-1521.
    • (1997) J. Lipid Res. , vol.38 , pp. 1503-1521
    • Fielding, C.J.1    Fielding, P.E.2
  • 13
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by cross-linking
    • Friedrichson, T., and T.V. Kurzchalia. 1998. Microdomains of GPI-anchored proteins in living cells revealed by cross-linking. Nature. 394:802-805.
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 15
    • 0032931281 scopus 로고    scopus 로고
    • Importance of CD44 variant isoforms in mouse models for inflammatory bowel disease
    • F. Melchers and M. Potter, editors
    • Günthert, U. 1999. Importance of CD44 variant isoforms in mouse models for inflammatory bowel disease. In CTMI 246: Mechanisms of B Cell Neoplasia 1998. F. Melchers and M. Potter, editors. 307-313.
    • (1999) CTMI 246: Mechanisms of B Cell Neoplasia 1998 , pp. 307-313
    • Günthert, U.1
  • 16
    • 0027534927 scopus 로고
    • Clathrin and HA2 adaptors: Effects of potassium depletion, hypertonic medium, and cytosol acidification
    • Hansen, S.H., K. Sandvig, and B. van Deurs. 1993. Clathrin and HA2 adaptors: effects of potassium depletion, hypertonic medium, and cytosol acidification. J. Cell Biol. 121:61-72.
    • (1993) J. Cell Biol. , vol.121 , pp. 61-72
    • Hansen, S.H.1    Sandvig, K.2    Van Deurs, B.3
  • 17
    • 0027426724 scopus 로고
    • The subcellular distribution of early endosomes is affected by the annexin II2p112 complex
    • Harder, T., and V. Gerke. 1993. The subcellular distribution of early endosomes is affected by the annexin II2p112 complex. J. Cell Biol. 123:1119-1132.
    • (1993) J. Cell Biol. , vol.123 , pp. 1119-1132
    • Harder, T.1    Gerke, V.2
  • 19
    • 0030899412 scopus 로고    scopus 로고
    • Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol
    • Harder, T., R. Kellner, R.G. Parton, and J. Gruenberg. 1997. Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol. Mol. Biol. Cell. 8:533-545.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 533-545
    • Harder, T.1    Kellner, R.2    Parton, R.G.3    Gruenberg, J.4
  • 20
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae. DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • Harder, T., and K. Simons. 1997. Caveolae. DIGs, and the dynamics of sphingolipid-cholesterol microdomains. Curr. Opin. Cell Biol. 9:534-542.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 21
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., P. Scheiffele, P. Verkade, and K. Simons. 1998. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141:929-942.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 22
    • 0018185320 scopus 로고
    • The picomole determination of free and total cholesterol in cells in culture
    • Heider, J.G., and R.L. Boyett. 1978. The picomole determination of free and total cholesterol in cells in culture. J. Lipid. Res. 19:514-518.
    • (1978) J. Lipid. Res. , vol.19 , pp. 514-518
    • Heider, J.G.1    Boyett, R.L.2
  • 23
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao, M., N. Sato, T. Kondo, S. Yonemura, M. Monden, T. Sasaki, Y. Takai, and S. Tsukita. 1996. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J. Cell Biol. 135: 37-51.
    • (1996) J. Cell Biol. , vol.135 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6    Takai, Y.7    Tsukita, S.8
  • 25
    • 0032177419 scopus 로고    scopus 로고
    • Protein and lipid sorting from the trans-Golgi network to the plasma membrane in polarized cells
    • Ikonen, E., and K. Simons. 1998. Protein and lipid sorting from the trans-Golgi network to the plasma membrane in polarized cells. Semin. Cell Devel. Biol. 9:503-509.
    • (1998) Semin. Cell Devel. Biol. , vol.9 , pp. 503-509
    • Ikonen, E.1    Simons, K.2
  • 26
    • 0032525106 scopus 로고    scopus 로고
    • CD44 selectively associates with active Src family protein tyrosine kinases Lck and Fyn in glycosphin-golipid-rich plasma membrane domains of human peripheral blood lymphocytes
    • Ilangumaran, S., A. Briol, and D. Hoessli. 1998. CD44 selectively associates with active Src family protein tyrosine kinases Lck and Fyn in glycosphin-golipid-rich plasma membrane domains of human peripheral blood lymphocytes. Blood. 91:3901-3908.
    • (1998) Blood , vol.91 , pp. 3901-3908
    • Ilangumaran, S.1    Briol, A.2    Hoessli, D.3
  • 27
    • 0032532271 scopus 로고    scopus 로고
    • Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane
    • Ilangumaran, S., and D. Hoessli. 1998. Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane. Biochem. J. 335:433-440.
    • (1998) Biochem. J. , vol.335 , pp. 433-440
    • Ilangumaran, S.1    Hoessli, D.2
  • 28
    • 0027930281 scopus 로고
    • The role of the cytoplasmic domain in regulating CD44 function
    • Isacke, C.M. 1994. The role of the cytoplasmic domain in regulating CD44 function. J. Cell Sci. 107:2353-2359.
    • (1994) J. Cell Sci. , vol.107 , pp. 2353-2359
    • Isacke, C.M.1
  • 29
    • 0021680651 scopus 로고
    • Lateral diffusion of an 80,000-dalton glycoprotein in the plasma membrane of murine fibroblasts: Relationships to cell structure and function
    • Jacobson, K., D. O'Dell, and J.T. August. 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.
    • (1984) J. Cell Biol. , vol.99 , pp. 1624-1633
    • Jacobson, K.1    O'Dell, D.2    August, J.T.3
  • 30
    • 0032514214 scopus 로고    scopus 로고
    • Effects of regulated expression of mutant RhoA and Racl small GTPases on the development of epithelial (MDCK) cell polarity
    • Jou, T.S., and W.J. Nelson. 1998. Effects of regulated expression of mutant RhoA and Racl small GTPases on the development of epithelial (MDCK) cell polarity. J. Cell Biol. 142:85-100.
    • (1998) J. Cell Biol. , vol.142 , pp. 85-100
    • Jou, T.S.1    Nelson, W.J.2
  • 31
    • 0025992141 scopus 로고
    • Dual-view microscopy with a single camera: Real-time imaging of molecular orientations and calcium
    • Kinosita, K., H. Itoh, and S. Ishiwata. 1991. Dual-view microscopy with a single camera: real-time imaging of molecular orientations and calcium. J. Cell Biol. 115:67-73.
    • (1991) J. Cell Biol. , vol.115 , pp. 67-73
    • Kinosita, K.1    Itoh, H.2    Ishiwata, S.3
  • 32
    • 0028812541 scopus 로고
    • Alteration of the myometrial plasma membrane cholesterol content with beta-cyclodextrin modulates the binding affinity of the oxytocin receptor
    • Klein, U., G. Gimpl, and F. Fahrenholz. 1995. Alteration of the myometrial plasma membrane cholesterol content with beta-cyclodextrin modulates the binding affinity of the oxytocin receptor. Biochemistry. 34:13784-13793.
    • (1995) Biochemistry , vol.34 , pp. 13784-13793
    • Klein, U.1    Gimpl, G.2    Fahrenholz, F.3
  • 33
    • 0026623542 scopus 로고
    • Protein-protein interaction studied by site-directed mutagenesis. Characterization of the annexin II-binding site on p11, a member of the S100 protein family
    • Kube, E., T. Becker, K. Weber, and V. Gerke. 1992. Protein-protein interaction studied by site-directed mutagenesis. Characterization of the annexin II-binding site on p11, a member of the S100 protein family. J. Biol. Chem. 267: 14175-14182.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14175-14182
    • Kube, E.1    Becker, T.2    Weber, K.3    Gerke, V.4
  • 34
    • 0023603591 scopus 로고
    • The hyaluronate receptor is associated with actin filaments
    • Lacy, B.E., and C.B. Underhill. 1987. The hyaluronate receptor is associated with actin filaments. J. Cell Biol. 105:1395-1404.
    • (1987) J. Cell Biol. , vol.105 , pp. 1395-1404
    • Lacy, B.E.1    Underhill, C.B.2
  • 35
    • 0032555901 scopus 로고    scopus 로고
    • Annexin XIIIb associates with lipid microdomains to function in apical delivery
    • Lafont, F., S. Lecat, P. Verkade, and K. Simons. 1998. Annexin XIIIb associates with lipid microdomains to function in apical delivery. J. Cell Biol. 142:1413-1427.
    • (1998) J. Cell Biol. , vol.142 , pp. 1413-1427
    • Lafont, F.1    Lecat, S.2    Verkade, P.3    Simons, K.4
  • 36
    • 0027197441 scopus 로고
    • Antibody-induced activation of the hyaluronan receptor function of CD44 requires multivalent binding by antibody
    • Lesley, J., P.W. Kincade, and R. Hyman. 1993. Antibody-induced activation of the hyaluronan receptor function of CD44 requires multivalent binding by antibody. Eur. J. Immunol. 23:1902-1909.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 1902-1909
    • Lesley, J.1    Kincade, P.W.2    Hyman, R.3
  • 38
    • 0031571729 scopus 로고    scopus 로고
    • Phorbol myristate acetate stimulates the dimerization of CD44 involving a cysteine in the transmembrane domain
    • Liu, D., and M.S. Sy. 1997. Phorbol myristate acetate stimulates the dimerization of CD44 involving a cysteine in the transmembrane domain. J. Immunol. 159:2702-2711.
    • (1997) J. Immunol. , vol.159 , pp. 2702-2711
    • Liu, D.1    Sy, M.S.2
  • 39
    • 0030872949 scopus 로고    scopus 로고
    • Rho- And rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    • Mackay, D.J., F. Esch, H. Furthmayr, and A. Hall. 1997. Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. J. Cell Biol. 138:927-938.
    • (1997) J. Cell Biol. , vol.138 , pp. 927-938
    • Mackay, D.J.1    Esch, F.2    Furthmayr, H.3    Hall, A.4
  • 40
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • Mayor, S., K. Rothberg, and F. Maxfield. 1994. Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking. Science. 264:1948-1951.
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.2    Maxfield, F.3
  • 41
    • 15844431258 scopus 로고    scopus 로고
    • Localization of epidermal growth factor-stimulated Ras/Raf-I interaction to caveolae membrane
    • Mineo, C., G.L. James, E.J. Smart, and R.G.W. Anderson. 1996. Localization of epidermal growth factor-stimulated Ras/Raf-I interaction to caveolae membrane. J. Biol. Chem. 271:11930-11935.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11930-11935
    • Mineo, C.1    James, G.L.2    Smart, E.J.3    Anderson, R.G.W.4
  • 42
    • 0030936823 scopus 로고    scopus 로고
    • Reversible palmitoylation of signaling proteins
    • Mumby, S. 1997. Reversible palmitoylation of signaling proteins. Curr. Opin. Cell. Biol. 9:148-154.
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , pp. 148-154
    • Mumby, S.1
  • 43
    • 0030966842 scopus 로고    scopus 로고
    • CD44: Structure, function and association with the malignant process
    • Naot, D. 1997. CD44: structure, function and association with the malignant process. Adv. Cancer Res. 71:241-319.
    • (1997) Adv. Cancer Res. , vol.71 , pp. 241-319
    • Naot, D.1
  • 44
    • 0027238315 scopus 로고
    • The cytoplasmic tail of CD44 is required for basolateral localization in epithelial MDCK cells but does not mediate association with the detergent-insoluble cytoskeleton of fibroblasts
    • Neame, S.J., and C.M. Isacke. 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 of fibroblasts. J. Cell Biol. 121:1299-1310.
    • (1993) J. Cell Biol. , vol.121 , pp. 1299-1310
    • Neame, S.J.1    Isacke, C.M.2
  • 45
    • 0029156668 scopus 로고
    • CD44 exhibits a cell type dependent interaction with triton X-100 insoluble, lipid rich, plasma membrane domains
    • Neame, S.J., C.R. Uff, H. Sheikh, S.C. Wheatley, and C.M. Isacke. 1995. CD44 exhibits a cell type dependent interaction with triton X-100 insoluble, lipid rich, plasma membrane domains. J. Cell Sci. 108:3127-3135.
    • (1995) J. Cell Sci. , vol.108 , pp. 3127-3135
    • Neame, S.J.1    Uff, C.R.2    Sheikh, H.3    Wheatley, S.C.4    Isacke, C.M.5
  • 46
    • 0031750101 scopus 로고    scopus 로고
    • Filipin-dependent inhibition of cholera toxin: Evidence for toxin internalization and activation through caveolae-like domains
    • Orlandi, P.A., and P.H. Fishman. 1998. Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains. J. Cell Biol. 141:905-915.
    • (1998) J. Cell Biol. , vol.141 , pp. 905-915
    • Orlandi, P.A.1    Fishman, P.H.2
  • 47
    • 0029147426 scopus 로고
    • Digging into caveolae
    • Parton, R.G., and K. Simons. 1995. Digging into caveolae. Science. 269:1398-1399.
    • (1995) Science , vol.269 , pp. 1398-1399
    • Parton, R.G.1    Simons, K.2
  • 48
  • 49
    • 0028922840 scopus 로고
    • Transmembrane domain of CD44 is required for its detergent insolubility in fibroblasts
    • Perschl, A., J. Lesley, N. English, R. Hyman, and I. Trowbridge. 1995a. Transmembrane domain of CD44 is required for its detergent insolubility in fibroblasts. J. Cell Sci. 108:1033-1041.
    • (1995) J. Cell Sci. , vol.108 , pp. 1033-1041
    • Perschl, A.1    Lesley, J.2    English, N.3    Hyman, R.4    Trowbridge, I.5
  • 51
    • 0001331341 scopus 로고    scopus 로고
    • The CD44 protein family: Roles in embryogenesis and tumor progression
    • Ponta, H., and P. Herrlich. 1998. The CD44 protein family: roles in embryogenesis and tumor progression. Front. Biosci. 3:650-656.
    • (1998) Front. Biosci. , vol.3 , pp. 650-656
    • Ponta, H.1    Herrlich, P.2
  • 52
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A.J., and A. Hall. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 53
    • 0028145334 scopus 로고
    • Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction
    • Rodgers, W., B. Crise, and J.K. Rose. 1994. Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction. Mol. Cell. Biol. 14:5384-5391.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5384-5391
    • Rodgers, W.1    Crise, B.2    Rose, J.K.3
  • 54
    • 0029142235 scopus 로고
    • CD44 isoforms during differentiation and development
    • Ruiz, P., C. Schwärzler, and U. Günthert. 1995. CD44 isoforms during differentiation and development. Bioessays. 17:17-24.
    • (1995) Bioessays , vol.17 , pp. 17-24
    • Ruiz, P.1    Schwärzler, C.2    Günthert, U.3
  • 55
    • 0031765341 scopus 로고    scopus 로고
    • Role of plasmalemmal caveolin in signal transduction
    • Shaul, P.W., and R.G. Anderson. 1998. Role of plasmalemmal caveolin in signal transduction. Am. J. Physiol. 275:843-851.
    • (1998) Am. J. Physiol. , vol.275 , pp. 843-851
    • Shaul, P.W.1    Anderson, R.G.2
  • 56
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele, P., M.G. Roth, and K. Simons. 1997. Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO (Eur. Mol. Biol. Organ.) J. 16:5501-5508.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 58
    • 0027997787 scopus 로고
    • Filipin-sensitive caveolae-mediated transport in endothelium: Reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules
    • Schnitzer, J.E., P. Oh, E. Pinney, and J. Allard. 1994. Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules. J. Cell Biol. 127: 1217-1232.
    • (1994) J. Cell Biol. , vol.127 , pp. 1217-1232
    • Schnitzer, J.E.1    Oh, P.2    Pinney, E.3    Allard, J.4
  • 59
    • 17544383706 scopus 로고    scopus 로고
    • A di-hydrophobic Leu-Val motif regulates the basolateral localization of CD44 in polarized Madin-Darby canine kidney epithelial cells
    • Sheikh, H., and C.M. Isacke. 1996. A di-hydrophobic Leu-Val motif regulates the basolateral localization of CD44 in polarized Madin-Darby canine kidney epithelial cells. J. Biol. Chem. 271:12185-12190.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12185-12190
    • Sheikh, H.1    Isacke, C.M.2
  • 60
    • 0028175989 scopus 로고
    • Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae
    • Shenoy-Scaria, A.M., D.J. Dietzen, J. Kwong, D.C. Link, and D.M. Lublin. 1994. Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae. J. Cell Biol. 126:353-363.
    • (1994) J. Cell Biol. , vol.126 , pp. 353-363
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 61
    • 0029825416 scopus 로고    scopus 로고
    • Regulated clustering of variant CD44 proteins increases their hyaluronate binding capacity
    • Sleeman, W., M. Hofmann, J. Moll, P. Herrlich, and H. Ponta. 1996. Regulated clustering of variant CD44 proteins increases their hyaluronate binding capacity. J. Cell Biol. 135:1139-1150.
    • (1996) J. Cell Biol. , vol.135 , pp. 1139-1150
    • Sleeman, W.1    Hofmann, M.2    Moll, J.3    Herrlich, P.4    Ponta, H.5
  • 62
    • 0029743064 scopus 로고    scopus 로고
    • Clustered folate receptors deliver 5-methyltetrahydrofolate to cytoplasm of MA104 cells
    • Smart, E.J., C. Mineo, and R.G. Anderson. 1996. Clustered folate receptors deliver 5-methyltetrahydrofolate to cytoplasm of MA104 cells. J. Cell Biol. 134: 1169-1177.
    • (1996) J. Cell Biol. , vol.134 , pp. 1169-1177
    • Smart, E.J.1    Mineo, C.2    Anderson, R.G.3
  • 63
    • 0028941257 scopus 로고
    • Effects of CapG overexpression on agonist-induced motility and second messenger generation
    • Sun, H.Q., K. Kwiatkowska, D.C. Wooten, and H.L. Yin. 1995. Effects of CapG overexpression on agonist-induced motility and second messenger generation. J. Cell Biol. 129:147-156.
    • (1995) J. Cell Biol. , vol.129 , pp. 147-156
    • Sun, H.Q.1    Kwiatkowska, K.2    Wooten, D.C.3    Yin, H.L.4
  • 64
    • 0030846295 scopus 로고    scopus 로고
    • Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
    • Takahashi, K., T. Sasaki, A. Mammoto, K. Takaishi, T. Kameyama, S. Tsukita, and Y. Takai. 1997. Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. J. Biol. Chem. 272:23371-23375.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23371-23375
    • Takahashi, K.1    Sasaki, T.2    Mammoto, A.3    Takaishi, K.4    Kameyama, T.5    Tsukita, S.6    Takai, Y.7
  • 65
    • 0027094236 scopus 로고
    • The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- And Ca(2+)-binding sites
    • Thiel, C., M. Osborn, and V. Gerke. 1992. The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-binding sites. J. Cell Sci. 103:733-742.
    • (1992) J. Cell Sci. , vol.103 , pp. 733-742
    • Thiel, C.1    Osborn, M.2    Gerke, V.3
  • 66
    • 0031818723 scopus 로고    scopus 로고
    • Role of caveolae in cholesterol transport in arterial smooth muscle cells exposed to lipoproteins in vitro and in vivo
    • Thyberg, J., F. Calara, P. Dimayuga, J. Nilsson, and J. Regnstrom. 1998. Role of caveolae in cholesterol transport in arterial smooth muscle cells exposed to lipoproteins in vitro and in vivo. Lab. Invest. 78:825-837.
    • (1998) Lab. Invest. , vol.78 , pp. 825-837
    • Thyberg, J.1    Calara, F.2    Dimayuga, P.3    Nilsson, J.4    Regnstrom, J.5
  • 67
    • 0032513038 scopus 로고    scopus 로고
    • Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking
    • Uittenbogaard, A., Y. Ying, and E.J. Smart. 1998. Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking. J. Biol. Chem. 273:6525-6532.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6525-6532
    • Uittenbogaard, A.1    Ying, Y.2    Smart, E.J.3
  • 68
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R., and S. Mayor, 1998. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature. 394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 69
    • 0032483575 scopus 로고    scopus 로고
    • A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth
    • Wary, K.K., A. Mariotti, C. Zurzolo, and F.G. Giancotti. 1998. A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth. Cell. 94:625-634.
    • (1998) Cell , vol.94 , pp. 625-634
    • Wary, K.K.1    Mariotti, A.2    Zurzolo, C.3    Giancotti, F.G.4
  • 70
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel, D., and U.I. Flügge. 1984. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138:141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.