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Volumn 1, Issue 2, 1999, Pages 98-105

Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains

Author keywords

[No Author keywords available]

Indexed keywords

CAV1 PROTEIN, MOUSE; CAVEOLIN; CAVEOLIN 1; CHOLESTEROL; MEMBRANE LIPID; MEMBRANE PROTEIN; PROTEIN P21; RECOMBINANT PROTEIN;

EID: 0033145517     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/10067     Document Type: Article
Times cited : (403)

References (50)
  • 1
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock, J. F., Magee, A. I., Childs, J. E. & Marshall, C. J. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57, 1167-1177 (1989).
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 2
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • Hancock, J. F., Paterson, H. & Marshall, C. J. A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane. Cell 63, 133-139 (1990).
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 3
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • Resh, M. Myristylation and palmitylation of Src family members: the fats of the matter. Cell 76, 411-413 (1994).
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.1
  • 6
    • 0345135149 scopus 로고    scopus 로고
    • K-Ras is an essential gene in the mouse with partial functional overlap with N-Ras
    • Johnson, L. et al. K-Ras is an essential gene in the mouse with partial functional overlap with N-Ras. Genes Dev. 11, 2468-2481 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 2468-2481
    • Johnson, L.1
  • 7
    • 0024376173 scopus 로고
    • Ras oncogenes in human cancer: A review
    • Bos, J. L. ras oncogenes in human cancer: a review. Cancer Res. 49, 4682-4689 (1989).
    • (1989) Cancer Res. , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 8
    • 0031917171 scopus 로고    scopus 로고
    • Ras-GRF activates Ha-Ras, but not N-Ras or K-Ras 4B, protein in vivo
    • Jones, M. K. & Jackson, J. H. Ras-GRF activates Ha-Ras, but not N-Ras or K-Ras 4B, protein in vivo. J. Biol. Chem. 273, 1782-1787 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 1782-1787
    • Jones, M.K.1    Jackson, J.H.2
  • 9
    • 0032508517 scopus 로고    scopus 로고
    • Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase
    • Van, J., Roy, S., Apolloni, A., Lane, A. & Hancock, J. F. Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase. J. Biol. Chem. 273, 24052-24056 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 24052-24056
    • Van, J.1    Roy, S.2    Apolloni, A.3    Lane, A.4    Hancock, J.F.5
  • 10
    • 0032546232 scopus 로고    scopus 로고
    • Ha-ras and N-Ras regulate MAPK activity by distinct mechanisms in vivo
    • Hamilton, M. & Wolfman, A. Ha-ras and N-Ras regulate MAPK activity by distinct mechanisms in vivo. Oncogene 16, 1417-1428 (1998).
    • (1998) Oncogene , vol.16 , pp. 1417-1428
    • Hamilton, M.1    Wolfman, A.2
  • 11
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in membranes
    • Simons, K. & Ikonen, E. Functional rafts in membranes. Nature 387, 569-572 (1997).
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 12
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: What physical studies of model membranes reveal
    • Brown, R. E. Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J. Cell Sci. 111, 1-9 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 1-9
    • Brown, R.E.1
  • 13
    • 0029147426 scopus 로고
    • Digging into caveolae
    • Parton, R. G. & Simons, K. Digging into caveolae. Science 269, 1398-1399 (1995).
    • (1995) Science , vol.269 , pp. 1398-1399
    • Parton, R.G.1    Simons, K.2
  • 14
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson, R. G. The caveolae membrane system. Annu. Rev. Biochem. 67, 199-225 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199-225
    • Anderson, R.G.1
  • 15
    • 0028885614 scopus 로고
    • VIP21/caveolin is a cholesterol-binding protein
    • Murata, M. et al. VIP21/caveolin is a cholesterol-binding protein. Proc. Natl Acad. Sci. USA 92, 10339-10343 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10339-10343
    • Murata, M.1
  • 16
    • 0030809601 scopus 로고    scopus 로고
    • Intracellular cholesterol transport
    • Fielding, C. J. & Fielding, P. E. Intracellular cholesterol transport. J. Lipid Res. 38, 1503-1521 (1997).
    • (1997) J. Lipid Res. , vol.38 , pp. 1503-1521
    • Fielding, C.J.1    Fielding, P.E.2
  • 17
    • 0031888035 scopus 로고    scopus 로고
    • Regulation of caveolin and caveolae by cholesterol in MDCK cells
    • Hailstones, D., Sleer, L. S., Parton, R. G. & Stanley, K. K. Regulation of caveolin and caveolae by cholesterol in MDCK cells. J. Lipid Res. 39, 369-379 (1998).
    • (1998) J. Lipid Res. , vol.39 , pp. 369-379
    • Hailstones, D.1    Sleer, L.S.2    Parton, R.G.3    Stanley, K.K.4
  • 18
    • 0030970279 scopus 로고    scopus 로고
    • Caveolin mRNA levels are up-regulated by free cholesterol and down-regulated by oxysterols in fibroblast monolayers
    • Fielding, C. J., Bist, A. & Fielding, P. E. Caveolin mRNA levels are up-regulated by free cholesterol and down-regulated by oxysterols in fibroblast monolayers. Proc. Natl Acad. Sci. USA 94, 3753-3758 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3753-3758
    • Fielding, C.J.1    Bist, A.2    Fielding, P.E.3
  • 19
    • 0029799891 scopus 로고    scopus 로고
    • A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane
    • Smart, E. J., Ying, Y., Donzell, W. C. & Anderson, R. G. A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane. J. Biol. Chem. 271, 29427-29435 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 29427-29435
    • Smart, E.J.1    Ying, Y.2    Donzell, W.C.3    Anderson, R.G.4
  • 20
    • 0030666672 scopus 로고    scopus 로고
    • Altered expression of caveolin-1 and increased cholesterol in detergent insoluble membrane fractions from liver in mice with Niemann-Pick disease type C
    • Garver, W. S. et al. Altered expression of caveolin-1 and increased cholesterol in detergent insoluble membrane fractions from liver in mice with Niemann-Pick disease type C. Biochim. Biophys. Acta 1361, 272-280 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1361 , pp. 272-280
    • Garver, W.S.1
  • 21
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing "preassembled signalling complexes" at the plasma membrane
    • Okamoto, T., Schlegel, A., Scherer, P. E. & Lisanti, M. P. Caveolins, a family of scaffolding proteins for organizing "preassembled signalling complexes" at the plasma membrane. J. Biol. Chem. 273, 5419-5422 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 22
    • 0030936016 scopus 로고    scopus 로고
    • Organized endothelial cell surface signal transduction in caveolae distinct from glycosylphosphatidylinositol-anchored protein microdomains
    • Liu, J., Oh, P., Horner, T., Rogers, R. A. & Schnitzer, J. E. Organized endothelial cell surface signal transduction in caveolae distinct from glycosylphosphatidylinositol-anchored protein microdomains. J. Biol. Chem. 272, 7211-7222 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 7211-7222
    • Liu, J.1    Oh, P.2    Horner, T.3    Rogers, R.A.4    Schnitzer, J.E.5
  • 23
    • 0031470628 scopus 로고    scopus 로고
    • Platelet-derived growth factor activates mitogen-activated protein kinase in isolated caveolae
    • Liu, P., Ying, Y. & Anderson, R. G. Platelet-derived growth factor activates mitogen-activated protein kinase in isolated caveolae. Proc. Natl Acad. Sci. USA 94, 13666-13670 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 13666-13670
    • Liu, P.1    Ying, Y.2    Anderson, R.G.3
  • 24
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (Erk)
    • Furuchi, T. & Anderson, R. G. W. Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (Erk). J. Biol. Chem. 273, 21099-21104 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 21099-21104
    • Furuchi, T.1    Anderson, R.G.W.2
  • 25
    • 0028953271 scopus 로고
    • Reduction of caveolin and caveolae in oncogenically transformed cells
    • Koleske, A. J., Baltimore, D. & Lisanti, M. P. Reduction of caveolin and caveolae in oncogenically transformed cells. Proc. Natl Acad. Sci. USA 92, 1381-1385 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1381-1385
    • Koleske, A.J.1    Baltimore, D.2    Lisanti, M.P.3
  • 26
    • 0030960332 scopus 로고    scopus 로고
    • Recombinant expression of caveolin-1 in oncogenically transformed cells abrogates anchorage-independent growth
    • Engelman, J. A. et al. Recombinant expression of caveolin-1 in oncogenically transformed cells abrogates anchorage-independent growth. J. Biol. Chem. 272, 16374-16381 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 16374-16381
    • Engelman, J.A.1
  • 27
    • 0032538790 scopus 로고    scopus 로고
    • Targeted down regulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44MAP kinase cascade
    • Galbiati, F. et al. Targeted down regulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44MAP kinase cascade. EMBO J. 17, 6633-6648 (1998).
    • (1998) EMBO J. , vol.17 , pp. 6633-6648
    • Galbiati, F.1
  • 28
    • 0029987340 scopus 로고    scopus 로고
    • Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae
    • Anderson, H. A., Chen, Y. & Norkin, L. C. Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae. Mol. Biol. Cell 7, 1825-1834 (1996).
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 29
    • 0030745673 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules mediate association of SV40 with caveolae
    • Stang, E., Kartenbeck, J. & Parton, R. G. Major histocompatibility complex class I molecules mediate association of SV40 with caveolae. Mol. Biol. Cell 8, 47-57 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 47-57
    • Stang, E.1    Kartenbeck, J.2    Parton, R.G.3
  • 30
    • 0031862578 scopus 로고    scopus 로고
    • 14-3-3 potentiates Ras dependent Raf-1 activation in vitro and in vivo
    • Roy, S. et al. 14-3-3 potentiates Ras dependent Raf-1 activation in vitro and in vivo. Mol. Cell. Biol. 18, 3947-3955 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3947-3955
    • Roy, S.1
  • 31
    • 0028241533 scopus 로고
    • Activation of Raf as a result of recruitment to the plasma membrane
    • Stokoe, D., Macdonald, S. G., Cadwallader, K., Symons, M. & Hancock, J. F. Activation of Raf as a result of recruitment to the plasma membrane. Science 264, 1463-1467 (1994).
    • (1994) Science , vol.264 , pp. 1463-1467
    • Stokoe, D.1    Macdonald, S.G.2    Cadwallader, K.3    Symons, M.4    Hancock, J.F.5
  • 32
    • 0030561979 scopus 로고
    • M-caveolin, a muscle-specific caveolin-related protein
    • Way, M. & Parton, R. G. M-caveolin, a muscle-specific caveolin-related protein. FEBS Lett. 376, 108-112 (1995).
    • (1995) FEBS Lett. , vol.376 , pp. 108-112
    • Way, M.1    Parton, R.G.2
  • 33
    • 0027414646 scopus 로고
    • Caveolae and sorting in the trans-Golgi network of epithelial cells
    • Dupree, P., Parton, R. G., Raposo, G., Kurzchalia, T. V. & Simons, K. Caveolae and sorting in the trans-Golgi network of epithelial cells. EMBO J. 12, 1597-1605 (1993).
    • (1993) EMBO J. , vol.12 , pp. 1597-1605
    • Dupree, P.1    Parton, R.G.2    Raposo, G.3    Kurzchalia, T.V.4    Simons, K.5
  • 34
    • 0031054410 scopus 로고    scopus 로고
    • Targeting of an intestinal apical endosomal protein to endosomes in nonpolarized cells
    • Wilson, J. M. & Colton, T. L. Targeting of an intestinal apical endosomal protein to endosomes in nonpolarized cells. J. Cell Biol. 136, 319-330 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 319-330
    • Wilson, J.M.1    Colton, T.L.2
  • 35
    • 0031214104 scopus 로고    scopus 로고
    • Internalized plasma membrane cholesterol passes through an endosome compartment that is distinct from the acid vesicle-lysosome compartment
    • Porpaczy, Z., Tomasek, J. J. & Freeman, D. A. Internalized plasma membrane cholesterol passes through an endosome compartment that is distinct from the acid vesicle-lysosome compartment. Exp. Cell Res. 234, 217-224 1997).
    • (1997) Exp. Cell Res. , vol.234 , pp. 217-224
    • Porpaczy, Z.1    Tomasek, J.J.2    Freeman, D.A.3
  • 36
    • 0032509356 scopus 로고    scopus 로고
    • Separation of "glycosphingolipid signalling domain" from caveolin-containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signalling
    • Iwabuchi, K., Handa, K. & Hakomori, S. Separation of "glycosphingolipid signalling domain" from caveolin-containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signalling. J. Biol. Chem. 273, 33766-33773 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 33766-33773
    • Iwabuchi, K.1    Handa, K.2    Hakomori, S.3
  • 37
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., Scheiffele, P., Verkade, P. & Simons, K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141, 929-942 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 38
    • 0027269661 scopus 로고
    • The tyrosine kinase connection: How GPI-anchored proteins activate T cells
    • Brown, D. The tyrosine kinase connection: how GPI-anchored proteins activate T cells. Curr. Opin. Immunol. 5, 349-354 (1993).
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 349-354
    • Brown, D.1
  • 39
    • 0028196986 scopus 로고
    • Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers
    • Silvius, J. R. & l'Heureux, F. Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers. Biochemistry 33, 3014-3022 (1994).
    • (1994) Biochemistry , vol.33 , pp. 3014-3022
    • Silvius, J.R.1    L'Heureux, F.2
  • 40
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes:Simple physics, complicated biology
    • Murray, D., Ben-Tal, N., Honig, B. & McLaughlin, S. Electrostatic interaction of myristoylated proteins with membranes:simple physics, complicated biology. Structure 5, 985-989 (1997).
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 41
    • 0032486433 scopus 로고    scopus 로고
    • Teratogen-mediated inhibition of target tissue response to Shh signaling
    • Cooper, M. K., Porter, J. A., Young, K. E. & Beachy, P. A. Teratogen-mediated inhibition of target tissue response to Shh signaling. Science 280, 603-1607 (1998).
    • (1998) Science , vol.280 , pp. 603-1607
    • Cooper, M.K.1    Porter, J.A.2    Young, K.E.3    Beachy, P.A.4
  • 42
    • 0026037624 scopus 로고
    • A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins
    • Hancock, J. F., Cadwallader, K., Paterson, H. & Marshall, C. J. A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins. EMBO J. 10, 4033-4039 (1991).
    • (1991) EMBO J. , vol.10 , pp. 4033-4039
    • Hancock, J.F.1    Cadwallader, K.2    Paterson, H.3    Marshall, C.J.4
  • 43
    • 0030854042 scopus 로고    scopus 로고
    • Activity of plasma membrane recruited Raf-1 is regulated by Ras via the Raf zinc finger
    • Roy, S., Lane, A., Yan, J., McPherson, R. & Hancock, J. F. Activity of plasma membrane recruited Raf-1 is regulated by Ras via the Raf zinc finger. J. Biol. Chem. 272, 20139-20145 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 20139-20145
    • Roy, S.1    Lane, A.2    Yan, J.3    McPherson, R.4    Hancock, J.F.5
  • 44
    • 0024517745 scopus 로고
    • Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle function in vitro
    • Gruenberg, J., Griffiths, G. & Howell, K. E. Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle function in vitro. J. Cell Biol. 108, 1301-1316 (1989).
    • (1989) J. Cell Biol. , vol.108 , pp. 1301-1316
    • Gruenberg, J.1    Griffiths, G.2    Howell, K.E.3
  • 45
    • 0029030937 scopus 로고
    • EEA-1, an early endosome-associated protein: EEA-1 is a conserved a-helical peripheral membrane protein flanked by "cysteine fingers" and contains a calmodulin-binding IQ motif
    • Mu, F.-T. et al. EEA-1, an early endosome-associated protein: EEA-1 is a conserved a-helical peripheral membrane protein flanked by "cysteine fingers" and contains a calmodulin-binding IQ motif. J. Biol. Chem. 270, 13503-13511 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 13503-13511
    • Mu, F.-T.1
  • 46
    • 0032510559 scopus 로고    scopus 로고
    • A lipid antigen associated with the anti-phospholipid syndrome regulates endosome structure/function
    • Kobayashi, T., Stang, E., de Moerloose, P., Parton, R. G. & Gruenberg, J. A lipid antigen associated with the anti-phospholipid syndrome regulates endosome structure/function. Nature 392, 193-197 (1998).
    • (1998) Nature , vol.392 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    De Moerloose, P.3    Parton, R.G.4    Gruenberg, J.5
  • 47
    • 0031030664 scopus 로고    scopus 로고
    • Caveolin-3 associates with developing T-tubules during muscle differentiation
    • Parton, R. G., Way, M., Zorzi, N. & Stang, E. Caveolin-3 associates with developing T-tubules during muscle differentiation. J. Cell Biol. 136, 137-154 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 137-154
    • Parton, R.G.1    Way, M.2    Zorzi, N.3    Stang, E.4
  • 48
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich, O., Reinsch, S., Urbe, S., Zerial, M. & Parton, R. G. Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol. 135, 913-924 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 49
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains
    • Song, S. K. et al. Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains. J. Biol. Chem. 271, 9690-9697 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 9690-9697
    • Song, S.K.1
  • 50
    • 0033612537 scopus 로고    scopus 로고
    • Molecular Characterization of caveolin association with the Golgi complex; identification of a cis Golgi targeting domain in the caveolin molecule
    • in the press
    • Luetterforst, R., Stang, E., Zorzi, N., Carozzi, A., Way, M., and Parton, R.G. Molecular Characterization of caveolin association with the Golgi complex; identification of a cis Golgi targeting domain in the caveolin molecule. J. Cell Biol. (in the press).
    • J. Cell Biol.
    • Luetterforst, R.1    Stang, E.2    Zorzi, N.3    Carozzi, A.4    Way, M.5    Parton, R.G.6


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