메뉴 건너뛰기




Volumn 63, Issue 7-8, 2006, Pages 939-948

Caveolin-1 interacts with the chaperone complex TCP-1 and modulates its protein folding activity

Author keywords

Caveolin; Chaperone; Filamin; Folding; Insulin; TCP 1

Indexed keywords

ACTIN; CAVEOLIN 1; CHAPERONE; FILAMIN; INSULIN; TYROSINE;

EID: 33646583471     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5551-z     Document Type: Article
Times cited : (12)

References (41)
  • 1
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson R. G. (1998) The caveolae membrane system. Annu. Rev. Biochem. 67: 199-225
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199-225
    • Anderson, R.G.1
  • 2
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans L., Kartenbeck J. and Helenius A. (2001) Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat. Cell Biol. 3: 473-483
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 3
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans L., Puntener D. and Helenius A. (2002) Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 296: 535-539
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 4
    • 0034604515 scopus 로고    scopus 로고
    • Involvement of cellular caveolae in bacterial entry into mast cells
    • Shin J. S., Gao Z. and Abraham S. N. (2000) Involvement of cellular caveolae in bacterial entry into mast cells. Science 289: 785-788
    • (2000) Science , vol.289 , pp. 785-788
    • Shin, J.S.1    Gao, Z.2    Abraham, S.N.3
  • 5
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing 'pre-assembled signaling complexes' at the plasma membrane
    • Okamoto T., Schlegel A., Scherer P. E. and Lisanti M. P (1998) Caveolins, a family of scaffolding proteins for organizing 'pre-assembled signaling complexes' at the plasma membrane. J. Biol. Chem. 273: 5419-5422
    • (1998) J. Biol. Chem. , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 6
    • 0034667394 scopus 로고    scopus 로고
    • Caveolin-1 levels are down-regulated in human colon tumors and ectopic expression of caveolin-1 in colon carcinoma cell lines reduces cell tumorigenicity
    • Bender F. C., Reymond M. A., Bron C. and Quest A. F. (2000) Caveolin-1 levels are down-regulated in human colon tumors and ectopic expression of caveolin-1 in colon carcinoma cell lines reduces cell tumorigenicity. Cancer Res. 60: 5870-5878
    • (2000) Cancer Res. , vol.60 , pp. 5870-5878
    • Bender, F.C.1    Reymond, M.A.2    Bron, C.3    Quest, A.F.4
  • 7
    • 0034647940 scopus 로고    scopus 로고
    • A molecular dissection of caveolin-1 membrane attachment and oligomerization. Two separate regions of the caveolin-1 C-terminal domain mediate membrane binding and oligomer/oligomer interactions in vivo
    • Schlegel A. and Lisanti M. P. (2000) A molecular dissection of caveolin-1 membrane attachment and oligomerization. Two separate regions of the caveolin-1 C-terminal domain mediate membrane binding and oligomer/oligomer interactions in vivo. J. Biol. Chem. 275: 21605-21617
    • (2000) J. Biol. Chem. , vol.275 , pp. 21605-21617
    • Schlegel, A.1    Lisanti, M.P.2
  • 8
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases, Galpha 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. (1996) Src tyrosine kinases, Galpha 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: 29182-29190
    • (1996) J. Biol. Chem. , vol.271 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 9
    • 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. (1997) 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: 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
  • 10
    • 0037119387 scopus 로고    scopus 로고
    • The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1
    • Kimura A., Mora S., Shigematsu S., Pessin J. E. and Saltiel A. R. (2002) The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1. J. Biol. Chem. 277: 30153-30158
    • (2002) J. Biol. Chem. , vol.277 , pp. 30153-30158
    • Kimura, A.1    Mora, S.2    Shigematsu, S.3    Pessin, J.E.4    Saltiel, A.R.5
  • 11
    • 0037341849 scopus 로고    scopus 로고
    • c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14
    • Sanguinetti A. R. and Masticke C. C (2003) c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14. Cell Signal. 15: 289-298
    • (2003) Cell Signal. , vol.15 , pp. 289-298
    • Sanguinetti, A.R.1    Masticke, C.C.2
  • 12
    • 0033659710 scopus 로고    scopus 로고
    • Constitutive and growth factor-regulated phosphorylation of caveolin-1 occurs at the same site (Tyr-14) in vivo: Identification of a c-Src/Cav-1/Grb7 signaling cassette
    • Lee H., Volonte D., Galbiati F., Iyengar P., Lublin D. M., Bregman D. B. et al. (2000) Constitutive and growth factor-regulated phosphorylation of caveolin-1 occurs at the same site (Tyr-14) in vivo: identification of a c-Src/Cav-1/Grb7 signaling cassette. Mol. Endocrinol. 14: 1750-1775
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1750-1775
    • Lee, H.1    Volonte, D.2    Galbiati, F.3    Iyengar, P.4    Lublin, D.M.5    Bregman, D.B.6
  • 13
    • 0029003932 scopus 로고
    • Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution. Identification and epitope mapping of an isoform-specific monoclonal antibody probe
    • Scherer P. E., Tang Z., Chun M., Sargiacomo M., Lodish H. F. and Lisanti M. P. (1995) Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution. Identification and epitope mapping of an isoform-specific monoclonal antibody probe. J. Biol. Chem. 270: 16395-16401
    • (1995) J. Biol. Chem. , vol.270 , pp. 16395-16401
    • Scherer, P.E.1    Tang, Z.2    Chun, M.3    Sargiacomo, M.4    Lodish, H.F.5    Lisanti, M.P.6
  • 14
    • 0036151510 scopus 로고    scopus 로고
    • Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking
    • Thomsen P., Roepstorff K., Stahlhut M. and van Deurs B. (2002) Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking. Mol. Biol. Cell 13: 238-250
    • (2002) Mol. Biol. Cell , vol.13 , pp. 238-250
    • Thomsen, P.1    Roepstorff, K.2    Stahlhut, M.3    Van Deurs, B.4
  • 15
    • 0026683609 scopus 로고
    • T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
    • Lewis V. A., Hynes G. M., Zheng D., Saibil H. and Willison K. (1992) T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol. Nature 358: 249-252
    • (1992) Nature , vol.358 , pp. 249-252
    • Lewis, V.A.1    Hynes, G.M.2    Zheng, D.3    Saibil, H.4    Willison, K.5
  • 16
    • 0029980091 scopus 로고    scopus 로고
    • Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
    • Frydman J. and Hartl F. U. (1996) Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. Science 272: 1497-1502
    • (1996) Science , vol.272 , pp. 1497-1502
    • Frydman, J.1    Hartl, F.U.2
  • 17
    • 0036049583 scopus 로고    scopus 로고
    • Function and regulation of cytosolic molecular chaperone CCT
    • Kubota H. (2002) Function and regulation of cytosolic molecular chaperone CCT. Vitam. Horm. 65: 313-331
    • (2002) Vitam. Horm. , vol.65 , pp. 313-331
    • Kubota, H.1
  • 18
    • 0022510984 scopus 로고
    • Molecular cloning and sequence analysis of a haploid expressed gene encoding t complex polypeptide 1
    • Willison K. R., Dudley K. and Potter J. (1986) Molecular cloning and sequence analysis of a haploid expressed gene encoding t complex polypeptide 1. Cell 44: 727-738
    • (1986) Cell , vol.44 , pp. 727-738
    • Willison, K.R.1    Dudley, K.2    Potter, J.3
  • 19
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes beta-actin folding
    • Gao Y., Thomas J. O., Chow R. L., Lee G. H. and Cowan N. J. (1992) A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell 69: 1043-1050
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 21
    • 0033540034 scopus 로고    scopus 로고
    • Eukaryotic type II chaperonin CCT interacts with actin through specific subunits
    • Llorca O., McCormack E. A., Hynes G., Grantham J., Cordell J., Carrascosa J. L. et al. (1999) Eukaryotic type II chaperonin CCT interacts with actin through specific subunits. Nature 402: 693-696
    • (1999) Nature , vol.402 , pp. 693-696
    • Llorca, O.1    McCormack, E.A.2    Hynes, G.3    Grantham, J.4    Cordell, J.5    Carrascosa, J.L.6
  • 22
    • 0034669110 scopus 로고    scopus 로고
    • Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations
    • Llorca O., Martin-Benito J., Ritco-Vonsovici M., Grantham J., Hynes G. M., Willison K. R. et al. (2000) Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations. EMBO J. 19: 5971-5979
    • (2000) EMBO J. , vol.19 , pp. 5971-5979
    • Llorca, O.1    Martin-Benito, J.2    Ritco-Vonsovici, M.3    Grantham, J.4    Hynes, G.M.5    Willison, K.R.6
  • 23
    • 0035983515 scopus 로고    scopus 로고
    • Crystal structure of the CCT-gamma apical domain: Implications for substrate binding to the eukaryotic cytosolic chaperonin
    • Pappenberger G., Wilsher J. A., Roe S. M., Counsell D. J., Willison K. R. and Pearl L. H. (2002) Crystal structure of the CCT-gamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin. J. Mol. Biol. 318: 1367-1379
    • (2002) J. Mol. Biol. , vol.318 , pp. 1367-1379
    • Pappenberger, G.1    Wilsher, J.A.2    Roe, S.M.3    Counsell, D.J.4    Willison, K.R.5    Pearl, L.H.6
  • 24
    • 0036166283 scopus 로고    scopus 로고
    • Dynamic association of human insulin receptor with lipid rafts in cells lacking caveolae
    • Vainio S., Heino S., Mansson J. E., Fredman P., Kuismanen E., Vaarala O. et al. (2002) Dynamic association of human insulin receptor with lipid rafts in cells lacking caveolae. EMBO J. 3: 95-100
    • (2002) EMBO J. , vol.3 , pp. 95-100
    • Vainio, S.1    Heino, S.2    Mansson, J.E.3    Fredman, P.4    Kuismanen, E.5    Vaarala, O.6
  • 25
    • 0038711647 scopus 로고    scopus 로고
    • Interaction of filamin A with the insulin receptor alters insulin-dependent activation of the mitogen-activated protein kinase pathway
    • He H. J., Kole S., Kwon Y. K., Crow M. T. and Bernier M. (2003) Interaction of filamin A with the insulin receptor alters insulin-dependent activation of the mitogen-activated protein kinase pathway. J. Biol. Chem. 278: 27096-27104
    • (2003) J. Biol. Chem. , vol.278 , pp. 27096-27104
    • He, H.J.1    Kole, S.2    Kwon, Y.K.3    Crow, M.T.4    Bernier, M.5
  • 27
    • 0031807109 scopus 로고
    • Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis
    • Rabilloud T. (1992) Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis. Electrophoresis 19: 758-760
    • (1992) Electrophoresis , vol.19 , pp. 758-760
    • Rabilloud, T.1
  • 28
    • 0031149870 scopus 로고    scopus 로고
    • Colloidal silver staining of electroblotted proteins for high sensitivity peptide mapping by liquid chromatography-electrospray ionization tandem mass spectrometry
    • van Oostveen I., Ducret A. and Aebersold R. (1997) Colloidal silver staining of electroblotted proteins for high sensitivity peptide mapping by liquid chromatography-electrospray ionization tandem mass spectrometry. Anal. Biochem. 247: 310-318
    • (1997) Anal. Biochem. , vol.247 , pp. 310-318
    • Van Oostveen, I.1    Ducret, A.2    Aebersold, R.3
  • 29
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O. and Mann M. (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68: 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 30
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • 1994
    • Eng J. K., McCormack A. L. and Yates J. R. III (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 1994. 5: 976-989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 31
    • 0038035145 scopus 로고    scopus 로고
    • The beta1 and beta3 integrins promote T cell receptor-mediated cytotoxic T lymphocyte activation
    • Doucey M. A., Legler D. F., Faroudi M., Boucheron N., Baumgaertner P., Naeher D. et al. (2003) The beta1 and beta3 integrins promote T cell receptor-mediated cytotoxic T lymphocyte activation. J. Biol. Chem. 278: 26983-26991
    • (2003) J. Biol. Chem. , vol.278 , pp. 26983-26991
    • Doucey, M.A.1    Legler, D.F.2    Faroudi, M.3    Boucheron, N.4    Baumgaertner, P.5    Naeher, D.6
  • 32
    • 0000186456 scopus 로고    scopus 로고
    • Thermal unfolding of G-actin monitored with the DNase I-inhibition assay stabilities of actin isoforms
    • Schuler H., Lindberg U., Schutt C. E. and Karlsson R. (2000) Thermal unfolding of G-actin monitored with the DNase I-inhibition assay stabilities of actin isoforms. Eur. J. Biochem. 267: 476-486
    • (2000) Eur. J. Biochem. , vol.267 , pp. 476-486
    • Schuler, H.1    Lindberg, U.2    Schutt, C.E.3    Karlsson, R.4
  • 33
    • 0018038933 scopus 로고
    • Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I
    • Blikstad I., Markey F., Carlsson L., Persson T. and Lindberg U. (1978) Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I. Cell 15: 935-943
    • (1978) Cell , vol.15 , pp. 935-943
    • Blikstad, I.1    Markey, F.2    Carlsson, L.3    Persson, T.4    Lindberg, U.5
  • 34
    • 0034682847 scopus 로고    scopus 로고
    • Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation and rapid transport of cholesterol to caveolae
    • Uittenbogaard A. and Smart E. J. (2000) Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation and rapid transport of cholesterol to caveolae. J. Biol. Chem. 275: 25595-25599
    • (2000) J. Biol. Chem. , vol.275 , pp. 25595-25599
    • Uittenbogaard, A.1    Smart, E.J.2
  • 35
    • 0032513038 scopus 로고    scopus 로고
    • Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking
    • Uittenbogaard A., Ying Y. and Smart E. J. (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
  • 36
    • 0033973279 scopus 로고    scopus 로고
    • Identification of filamin as a novel ligand for caveolin-1: Evidence for the organization of caveolin-1-associated membrane domains by the actin cytoskeleton
    • Stahlhut M. and van Deurs B. (2000) Identification of filamin as a novel ligand for caveolin-1: evidence for the organization of caveolin-1-associated membrane domains by the actin cytoskeleton. Mol. Biol. Cell 11: 325-337
    • (2000) Mol. Biol. Cell , vol.11 , pp. 325-337
    • Stahlhut, M.1    Van Deurs, B.2
  • 37
    • 0034705567 scopus 로고    scopus 로고
    • Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of beta-actin
    • Hynes G. M. and Willison K. R. (2000) Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of beta-actin. J. Biol. Chem. 275: 18985-18994
    • (2000) J. Biol. Chem. , vol.275 , pp. 18985-18994
    • Hynes, G.M.1    Willison, K.R.2
  • 38
    • 0028370512 scopus 로고
    • Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin
    • Kubota H., Hynes G., Carne A., Ashworth A. and Willison K. (1994) Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin. Curr. Biol. 4: 89-99
    • (1994) Curr. Biol. , vol.4 , pp. 89-99
    • Kubota, H.1    Hynes, G.2    Carne, A.3    Ashworth, A.4    Willison, K.5
  • 39
    • 0028895618 scopus 로고
    • Antibody characterisation of two distinct conformations of the chaperonin-containing TCP-1 from mouse testis
    • Hynes G., Kubota H. and Willison K. R. (1995) Antibody characterisation of two distinct conformations of the chaperonin-containing TCP-1 from mouse testis. FEBS Lett. 358: 129-132
    • (1995) FEBS Lett. , vol.358 , pp. 129-132
    • Hynes, G.1    Kubota, H.2    Willison, K.R.3
  • 40
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • USA
    • Foster L. J., De Hoog C. L. and Mann M. (2003) Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc. Natl. Acad. Sci. USA 100: 5813-5818
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 41
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • Liu P., Rudick M. and Anderson R. G. (2002) Multiple functions of caveolin-1. J. Biol. Chem. 277: 41295-41298
    • (2002) J. Biol. Chem. , vol.277 , pp. 41295-41298
    • Liu, P.1    Rudick, M.2    Anderson, R.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.