메뉴 건너뛰기




Volumn 583, Issue 22, 2009, Pages 3681-3689

A conserved sequence in caveolin-1 is both necessary and sufficient for caveolin polarity and cell directional migration

Author keywords

Caveolin; Cell polarity; Directional migration

Indexed keywords

CAVEOLIN 1; CAVEOLIN 2; CAVEOLIN 3;

EID: 71749108981     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.10.055     Document Type: Article
Times cited : (14)

References (36)
  • 3
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science 279 (1998) 509-514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 4
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville S., and Hall A. Rho GTPases in cell biology. Nature 420 (2002) 629-635
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 5
    • 0041352963 scopus 로고    scopus 로고
    • Directional sensing requires G beta gamma-mediated PAK1 and PIX alpha-dependent activation of Cdc42
    • Li Z., Hannigan M., Mo Z., Liu B., Lu W., Wu Y., Smrcka A.V., Wu G., Li L., Liu M., et al. Directional sensing requires G beta gamma-mediated PAK1 and PIX alpha-dependent activation of Cdc42. Cell 114 (2003) 215-227
    • (2003) Cell , vol.114 , pp. 215-227
    • Li, Z.1    Hannigan, M.2    Mo, Z.3    Liu, B.4    Lu, W.5    Wu, Y.6    Smrcka, A.V.7    Wu, G.8    Li, L.9    Liu, M.10
  • 8
    • 15844401780 scopus 로고    scopus 로고
    • Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins
    • Song K.S., Scherer P.E., Tang Z.-L., Okamoto T., Li S., Chafel M., Chu C., Kohtz D.S., and Lisanti M.P. Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins. J. Biol. Chem. 271 (1996) 15160-15165
    • (1996) J. Biol. Chem. , vol.271 , pp. 15160-15165
    • Song, K.S.1    Scherer, P.E.2    Tang, Z.-L.3    Okamoto, T.4    Li, S.5    Chafel, M.6    Chu, C.7    Kohtz, D.S.8    Lisanti, M.P.9
  • 10
    • 0033965898 scopus 로고    scopus 로고
    • Caveolin 1-mediated regulation of receptor tyrosine kinase-associated phosphatidylinositol 3-kinase activity by ceramide
    • Zundel W., Swiersz L.M., and Giaccia A. Caveolin 1-mediated regulation of receptor tyrosine kinase-associated phosphatidylinositol 3-kinase activity by ceramide. Mol. Cell. Biol. 20 (2000) 1507-1514
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1507-1514
    • Zundel, W.1    Swiersz, L.M.2    Giaccia, A.3
  • 11
    • 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., Mariott I.A., Zurzolo C., and Giancotti F.G. A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth. Cell 94 (1998) 625-634
    • (1998) Cell , vol.94 , pp. 625-634
    • Wary, K.K.1    Mariott, I.A.2    Zurzolo, C.3    Giancotti, F.G.4
  • 12
    • 0344507516 scopus 로고    scopus 로고
    • A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling
    • Wei Y., Yang X., Liu Q., Wilkins J.A., and Chapman H.A. A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling. J. Cell Biol. 144 (1999) 1285-1294
    • (1999) J. Cell Biol. , vol.144 , pp. 1285-1294
    • Wei, Y.1    Yang, X.2    Liu, Q.3    Wilkins, J.A.4    Chapman, H.A.5
  • 13
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases, G alpha subunits and H-Ras share a common membrane-anchored scaffolding protein, Caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases
    • Li S., Couet J., and Lisanti M.P. Src tyrosine kinases, G alpha subunits and H-Ras share a common membrane-anchored scaffolding protein, Caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. J. Biol. Chem. 271 (1996) 29182-29190
    • (1996) J. Biol. Chem. , vol.271 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 14
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins
    • Couet J., Li S., Okamoto T., Ikezu T., and Lisanti M.P. Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins. J. Biol. Chem. 272 (1997) 6525-6533
    • (1997) J. Biol. Chem. , vol.272 , pp. 6525-6533
    • Couet, J.1    Li, S.2    Okamoto, T.3    Ikezu, T.4    Lisanti, M.P.5
  • 15
    • 34147159581 scopus 로고    scopus 로고
    • Identification of a novel domain at the N terminus of caveolin-1 that controls rear polarization of the protein and caveolae formation
    • Sun X.H., Flynn D.C., Castranova V., Millecchia L.L., Beardsley A.R., and Liu J. Identification of a novel domain at the N terminus of caveolin-1 that controls rear polarization of the protein and caveolae formation. J. Biol. Chem. 282 (2007) 7232-7241
    • (2007) J. Biol. Chem. , vol.282 , pp. 7232-7241
    • Sun, X.H.1    Flynn, D.C.2    Castranova, V.3    Millecchia, L.L.4    Beardsley, A.R.5    Liu, J.6
  • 16
    • 13544252448 scopus 로고    scopus 로고
    • Loss of caveolin-1 polarity impedes endothelial cell polarization and directional movement
    • Beardsley A., Fang K., Mertz H., Castranova V., Friend S., and Liu J. Loss of caveolin-1 polarity impedes endothelial cell polarization and directional movement. J. Biol. Chem. 280 (2005) 3541-3547
    • (2005) J. Biol. Chem. , vol.280 , pp. 3541-3547
    • Beardsley, A.1    Fang, K.2    Mertz, H.3    Castranova, V.4    Friend, S.5    Liu, J.6
  • 17
    • 0041969715 scopus 로고    scopus 로고
    • Differential caveolin-1 polarization in endothelial cells during migration in two and three dimensions
    • Parat M.O., Anand-Apte B., and Fox P.L. Differential caveolin-1 polarization in endothelial cells during migration in two and three dimensions. Mol. Biol. Cell 14 (2003) 3156-3168
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3156-3168
    • Parat, M.O.1    Anand-Apte, B.2    Fox, P.L.3
  • 20
    • 0034627824 scopus 로고    scopus 로고
    • Multiple domains in caveolin-1 control its intracellular traffic
    • Machleidt T., Li W.P., Liu P., and Anderson R.G. Multiple domains in caveolin-1 control its intracellular traffic. J. Cell Biol. 148 (2000) 17-28
    • (2000) J. Cell Biol. , vol.148 , pp. 17-28
    • Machleidt, T.1    Li, W.P.2    Liu, P.3    Anderson, R.G.4
  • 21
    • 0038313015 scopus 로고    scopus 로고
    • The phosphorylation of caveolin-2 on serines 23 and 36 modulates caveolin-1-dependent caveolae formation
    • Sowa G., Pypaert M., Fulton D., and Sessa W.C. The phosphorylation of caveolin-2 on serines 23 and 36 modulates caveolin-1-dependent caveolae formation. Proc. Natl. Acad. Sci. USA 100 (2003) 6511-6566
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6511-6566
    • Sowa, G.1    Pypaert, M.2    Fulton, D.3    Sessa, W.C.4
  • 24
    • 0031047967 scopus 로고    scopus 로고
    • Mutational analysis of the properties of caveolin-1. A novel role for the C-terminal domain in mediating homo-typic caveolin-caveolin interactions
    • Song K.S., Tang Z., Li S., and Lisanti M.P. Mutational analysis of the properties of caveolin-1. A novel role for the C-terminal domain in mediating homo-typic caveolin-caveolin interactions. J. Biol. Chem. 272 (1997) 4398-4403
    • (1997) J. Biol. Chem. , vol.272 , pp. 4398-4403
    • Song, K.S.1    Tang, Z.2    Li, S.3    Lisanti, M.P.4
  • 25
    • 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
    • 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. 145 (1999) 1443-1459
    • (1999) J. Cell Biol. , vol.145 , pp. 1443-1459
    • Luetterforst, R.1    Stang, E.2    Zorzi, N.3    Carozzi, A.4    Way, M.5    Parton, R.G.6
  • 26
    • 4644286390 scopus 로고    scopus 로고
    • Conformational defects slow Golgi exit, block oligomerization, and reduce raft affinity of caveolin-1 mutant proteins
    • Ren X., Ostermeyer A.G., Ramcharan L.T., Zeng Y., Lublin D.M., and Brown D.A. Conformational defects slow Golgi exit, block oligomerization, and reduce raft affinity of caveolin-1 mutant proteins. Mol. Biol. Cell 15 (2004) 4556-4567
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4556-4567
    • Ren, X.1    Ostermeyer, A.G.2    Ramcharan, L.T.3    Zeng, Y.4    Lublin, D.M.5    Brown, D.A.6
  • 29
    • 0035477544 scopus 로고    scopus 로고
    • Par-4 drives trafficking and activation of Fas and Fasl to induce prostate cancer cell apoptosis and tumor regression
    • Chakraborty M., Qiu S.G., Vasudevan K.M., and Rangnekar V.M. Par-4 drives trafficking and activation of Fas and Fasl to induce prostate cancer cell apoptosis and tumor regression. Cancer Res. 61 (2001) 7255-7263
    • (2001) Cancer Res. , vol.61 , pp. 7255-7263
    • Chakraborty, M.1    Qiu, S.G.2    Vasudevan, K.M.3    Rangnekar, V.M.4
  • 30
    • 35948986807 scopus 로고    scopus 로고
    • ZIPK: a unique case of murine-specific divergence of a conserved vertebrate gene
    • Shoval Y., Pietrokovski S., and Kimchi A. ZIPK: a unique case of murine-specific divergence of a conserved vertebrate gene. PLoS Genet. 3 (2007) 1884-1893
    • (2007) PLoS Genet. , vol.3 , pp. 1884-1893
    • Shoval, Y.1    Pietrokovski, S.2    Kimchi, A.3
  • 33
    • 0042733080 scopus 로고    scopus 로고
    • Initiation and transduction of stretch-induced RhoA and Rac1 activation through caveolae: cytoskeletal regulation of ERK translocation
    • Kawamura S., Miyamoto S., and Brown J.H. Initiation and transduction of stretch-induced RhoA and Rac1 activation through caveolae: cytoskeletal regulation of ERK translocation. J. Biol. Chem. 278 (2003) 31111-31117
    • (2003) J. Biol. Chem. , vol.278 , pp. 31111-31117
    • Kawamura, S.1    Miyamoto, S.2    Brown, J.H.3
  • 34
    • 33745831899 scopus 로고    scopus 로고
    • Caveolin-1 functions as a novel Cdc42 guanine nucleotide dissociation inhibitor in pancreatic beta-cells
    • Nevins A.K., and Thurmond D.C. Caveolin-1 functions as a novel Cdc42 guanine nucleotide dissociation inhibitor in pancreatic beta-cells. J. Biol. Chem. 281 (2006) 18961-18972
    • (2006) J. Biol. Chem. , vol.281 , pp. 18961-18972
    • Nevins, A.K.1    Thurmond, D.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.