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Volumn 16, Issue 2, 2011, Pages 173-179

Interactions between the actin filament capping and severing protein gelsolin and the molecular chaperone CCT: Evidence for nonclassical substrate interactions

Author keywords

Actin cytoskeleton; CCT; Gelsolin; Molecular chaperone

Indexed keywords

CHAPERONE; GELSOLIN; PROTEIN CCT; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 79951669713     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-010-0230-x     Document Type: Article
Times cited : (23)

References (30)
  • 1
    • 58749116660 scopus 로고    scopus 로고
    • Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin
    • 1:CAS:528:DC%2BD1cXhsFCitbjK 10.1098/rsif.2008.0185 18708324
    • GM Altschuler KR Willison 2008 Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin J R Soc Interface 5 1391 1408 1:CAS:528:DC%2BD1cXhsFCitbjK 10.1098/rsif.2008.0185 18708324
    • (2008) J R Soc Interface , vol.5 , pp. 1391-1408
    • Altschuler, G.M.1    Willison, K.R.2
  • 2
    • 0034635549 scopus 로고    scopus 로고
    • Gelsolin in complex with phosphatidylinositol 4,5-bisphosphate inhibits caspase-3 and -9 to retard apoptotic progression
    • DOI 10.1074/jbc.275.6.3761
    • TK Azuma K Koths L Flanagan D Kwiatkowski 2000 Gelsolin in complex with phosphatidylinositol4, 5-bisphosphate inhibits caspase-3 and -9 to retard apoptotic progression J Biol Chem 275 3761 3766 1:CAS:528:DC%2BD3cXht12hu70%3D 10.1074/jbc.275.6.3761 10660524 (Pubitemid 30094596)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 3761-3766
    • Azuma, T.1    Koths, K.2    Flanagan, L.3    Kwiatkowski, D.4
  • 3
    • 67649229560 scopus 로고    scopus 로고
    • Activities of the chaperonin containing TCP-1 (CCT): Implications for cell cycle progression and cytoskeletal organization
    • 1:CAS:528:DC%2BD1MXhvVyktLY%3D 10.1007/s12192-008-0057-x 18595008
    • KI Brackley J Grantham 2009 Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organization Cell Stress Chaperones 14 23 31 1:CAS:528:DC%2BD1MXhvVyktLY%3D 10.1007/s12192-008-0057-x 18595008
    • (2009) Cell Stress Chaperones , vol.14 , pp. 23-31
    • Brackley, K.I.1    Grantham, J.2
  • 4
    • 77449113481 scopus 로고    scopus 로고
    • Subunits of the chaperonin CCT interact with F-actin and influence cell shape and cytoskeletal assembly
    • 1:CAS:528:DC%2BC3cXhtlCmtro%3D 10.1016/j.yexcr.2009.11.003 19913534
    • KI Brackley J Grantham 2010 Subunits of the chaperonin CCT interact with F-actin and influence cell shape and cytoskeletal assembly Exp Cell Res 316 543 553 1:CAS:528:DC%2BC3cXhtlCmtro%3D 10.1016/j.yexcr.2009.11.003 19913534
    • (2010) Exp Cell Res , vol.316 , pp. 543-553
    • Brackley, K.I.1    Grantham, J.2
  • 5
    • 0030829385 scopus 로고    scopus 로고
    • The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation
    • DOI 10.1016/S0092-8674(00)80527-9
    • LD Burtnick EK Koepf J Grimes EY Jones DI Stuart PJ McLaughlin RC Robinson 1997 The crystal structure of plasma gelsolin: implications for actin severing, capping and nucleation Cell 90 661 670 1:CAS:528:DyaK2sXlvFKmtbs%3D 10.1016/S0092-8674(00)80527-9 9288746 (Pubitemid 27357958)
    • (1997) Cell , vol.90 , Issue.4 , pp. 661-670
    • Burtnick, L.D.1    Koepf, E.K.2    Grimes, J.3    Jones, E.Y.4    Stuart, D.I.5    McLaughlin, P.J.6    Robinson, R.C.7
  • 6
    • 12244289640 scopus 로고    scopus 로고
    • Gelsolin-induced epithelial cell invasion is dependent on Ras-Rac signaling
    • DOI 10.1093/emboj/cdf680
    • V De Corte E Bruyneel C Boucherie M Mareel J Vandekerckhove J Gettemans 2002 Gelsolin-induced epithelial cell invasion is dependent on Ras-Rac signaling EMBO J 21 6781 6790 10.1093/emboj/cdf680 12485999 (Pubitemid 36014550)
    • (2002) EMBO Journal , vol.21 , Issue.24 , pp. 6781-6790
    • De Corte, V.1    Bruyneel, E.2    Boucherie, C.3    Mareel, M.4    Vandekerckhove, J.5    Gettemans, J.6
  • 8
    • 79951674587 scopus 로고    scopus 로고
    • The eukaryotic chaperonin CCT (TRiC): Structure, mechanisms of actin and substrate diversity
    • P. Durante L. Colucci (eds). Nova Science New York
    • Grantham J (2010) The eukaryotic chaperonin CCT (TRiC): structure, mechanisms of actin and substrate diversity. In: Durante P, Colucci L (eds) Molecular chaperones: roles structures and mechanisms. Nova Science, New York
    • (2010) Molecular Chaperones: Roles Structures and Mechanisms
    • Grantham, J.1
  • 9
    • 0034681443 scopus 로고    scopus 로고
    • Partial occlusion of both cavities of the eukaryotic chaperonin with antibody has no effect upon the rates of β-actin or α-tubulin folding
    • DOI 10.1074/jbc.275.7.4587
    • J Grantham O Llorca JM Valpuesta KR Willison 2000 Partial occlusion of both cavities of the eukaryotic chaperonin with antibody has no effect upon the rates of beta-actin or alpha-tubulin folding J Biol Chem 275 4587 4591 1:CAS:528:DC%2BD3cXhsVyntb0%3D 10.1074/jbc.275.7.4587 10671484 (Pubitemid 30108841)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.7 , pp. 4587-4591
    • Grantham, J.1    Llorca, O.2    Valpuesta, J.M.3    Willison, K.R.4
  • 10
    • 0036665914 scopus 로고    scopus 로고
    • Eukaryotic chaperonin containing T-complex polypeptide 1 interacts with filamentous actin and reduces the initial rate of actin polymerization in vitro
    • DOI 10.1379/1466-1268(2002)007<0235:ECCTCP>2.0.CO;2
    • J Grantham LW Ruddock A Roobol MJ Carden 2002 Eukaryotic chaperonin containing T-complex polypeptide 1 interacts with filamentous actin and reduces the initial rate of actin polymerization in vitro Cell Stress Chaperones 7 235 242 1:CAS:528:DC%2BD38XptV2gs78%3D 10.1379/1466-1268(2002)007<0235: ECCTCP>2.0.CO;2 12482199 (Pubitemid 36135071)
    • (2002) Cell Stress and Chaperones , vol.7 , Issue.3 , pp. 235-242
    • Grantham, J.1    Ruddock, L.W.2    Roobol, A.3    Carden, M.J.4
  • 11
    • 33745246007 scopus 로고    scopus 로고
    • Substantial CCT activity is required for cell cycle progression and cytoskeletal organization in mammalian cells
    • DOI 10.1016/j.yexcr.2006.03.028, PII S0014482706001248
    • J Grantham KI Brackley KR Willison 2006 Substantial CCT activity is required for cell cycle progression and cytoskeletal organization in mammalian cells Exp Cell Res 312 2309 2324 1:CAS:528:DC%2BD28XmtlajsrY%3D 10.1016/j.yexcr.2006.03.028 16765944 (Pubitemid 43928947)
    • (2006) Experimental Cell Research , vol.312 , Issue.12 , pp. 2309-2324
    • Grantham, J.1    Brackley, K.I.2    Willison, K.R.3
  • 13
    • 0034705567 scopus 로고    scopus 로고
    • Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of β-actin
    • DOI 10.1074/jbc.M910297199
    • GM Hynes KR Willison 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 1:CAS:528:DC%2BD3cXksVGktb4%3D 10.1074/jbc.M910297199 10748209 (Pubitemid 30422864)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 18985-18994
    • Hynes, G.M.1    Willison, K.R.2
  • 14
    • 0032966363 scopus 로고    scopus 로고
    • Functions of gelsolin: Motility, signaling, apoptosis, cancer
    • DOI 10.1016/S0955-0674(99)80012-X
    • DJ Kwiatkowski 1999 Functions of gelsolin: motility, signaling, apoptosis, cancer Curr Opin Cell Biol 11 103 108 1:CAS:528:DyaK1MXhsFSnurs%3D 10.1016/S0955-0674(99)80012-X 10047530 (Pubitemid 29084137)
    • (1999) Current Opinion in Cell Biology , vol.11 , Issue.1 , pp. 103-108
    • Kwiatkowski, D.J.1
  • 15
    • 0022487183 scopus 로고
    • Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain
    • DJ Kwiatkowski TPO Stossel SH Orkin JE Mole HR Colten HL Yin 1986 Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicating actin-binding domain Nature 323 455 458 1:CAS:528:DyaL2sXhtlyqtA%3D%3D 10.1038/323455a0 3020431 (Pubitemid 16026275)
    • (1986) Nature , vol.323 , Issue.6087 , pp. 455-458
    • Kwiatkowski, D.J.1    Stossel, T.P.2    Orkin, S.H.3
  • 16
    • 0030842428 scopus 로고    scopus 로고
    • Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes
    • DOI 10.1093/emboj/16.14.4311
    • AK Liou KR Willison 1997 Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes EMBO J 16 4311 4316 1:CAS:528:DyaK2sXkvFeqtLc%3D 10.1093/emboj/16.14.4311 9250675 (Pubitemid 27298184)
    • (1997) EMBO Journal , vol.16 , Issue.14 , pp. 4311-4316
    • Liou, A.K.F.1    Willison, K.R.2
  • 19
    • 0035423032 scopus 로고    scopus 로고
    • The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin
    • DOI 10.1093/emboj/20.15.4065
    • O Llorca J Martin-Benito J Grantham M Ritco-Vonsovici KR Willison JL Carrascosa JM Valpuesta 2001 The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin EMBO J 20 4065 4075 1:CAS:528:DC%2BD3MXmtlChtrc%3D 10.1093/emboj/20.15.4065 11483510 (Pubitemid 32751823)
    • (2001) EMBO Journal , vol.20 , Issue.15 , pp. 4065-4075
    • Llorca, O.1    Martin-Benito, J.2    Grantham, J.3    Ritco-Vonsovici, M.4    Willison, K.R.5    Carrascosa, J.L.6    Valpuesta, J.M.7
  • 20
    • 0035783077 scopus 로고    scopus 로고
    • Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT
    • 1:CAS:528:DC%2BD3MXntFKqurY%3D 10.1006/jsbi.2001.4389 11580268
    • EA McCormack MJ Rohman KR Willison 2001 Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT J Struct Biol 135 185 197 1:CAS:528:DC%2BD3MXntFKqurY%3D 10.1006/jsbi.2001.4389 11580268
    • (2001) J Struct Biol , vol.135 , pp. 185-197
    • McCormack, E.A.1    Rohman, M.J.2    Willison, K.R.3
  • 21
    • 0035320252 scopus 로고    scopus 로고
    • Genes, chromatin, and breast cancer: An epigenetic tale
    • DOI 10.1023/A:1011356623442
    • LM Mielnicki HL Asch BB Asch 2001 Genes, chromatin, and breast cancer: an epigenetic tale J Mammary Gland Biol Neoplasia 6 169 182 1:STN:280: DC%2BD3MvlsFemsA%3D%3D 10.1023/A:1011356623442 11501577 (Pubitemid 39600508)
    • (2001) Journal of Mammary Gland Biology and Neoplasia , vol.6 , Issue.2 , pp. 169-182
    • Mielnicki, L.M.1    Asch, H.L.2    Asch, B.B.3
  • 22
    • 28844496012 scopus 로고    scopus 로고
    • Actin interacts with CCT via discrete binding sites: A binding transition-release model for CCT-mediated actin folding
    • DOI 10.1016/j.jmb.2005.10.051, PII S0022283605012982
    • K Neirynck D Waterschoot J Vandekerckhove C Ampe H Rommelaere 2006 Actin interacts with CCT via discrete binding sites: a binding transition-release model for CCT-mediated actin folding J Mol Biol 355 124 138 1:CAS:528: DC%2BD2MXhtlSjt7jN 10.1016/j.jmb.2005.10.051 16300788 (Pubitemid 41774144)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.1 , pp. 124-138
    • Neirynck, K.1    Waterschoot, D.2    Vandekerckhove, J.3    Ampe, C.4    Rommelaere, H.5
  • 23
    • 33745272858 scopus 로고    scopus 로고
    • Quantitative Actin Folding Reactions using Yeast CCT Purified via an Internal Tag in the CCT3/γ Subunit
    • DOI 10.1016/j.jmb.2006.05.003, PII S0022283606005699
    • G Pappenberger EA McCormack KR Willison 2006 Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/γ subunit J Mol Biol 360 484 496 1:CAS:528:DC%2BD28Xmt1yrt70%3D 10.1016/j.jmb.2006.05.003 16762366 (Pubitemid 43927828)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.2 , pp. 484-496
    • Pappenberger, G.1    McCormack, E.A.2    Willison, K.R.3
  • 24
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • DN Perkins DJ Pappin DM Creasy JS Cottrell 1999 Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 20 3551 3567 1:CAS:528:DC%2BD3cXhtF2ntw%3D%3D 10.1002/(SICI)1522-2683(19991201)20:18<3551::AID-ELPS3551>3.0.CO;2-2 10612281 (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 25
    • 0037105470 scopus 로고    scopus 로고
    • Tissue microarray analysis of cytoskeletal actin-associated biomarkers Gelsolin and E-cadherin in urothelial carcinoma
    • DOI 10.1002/cncr.10823
    • J Rao D Seligson H Visapaa S Horvath M Eeva K Michel A Pantuck A Belldegrun A Palotie 2002 Tissue microarray analysis of cytoskeletal actin-associated biomarkers gelsolin and E-cadherin in urothelial carcinoma Cancer 95 1247 1257 1:CAS:528:DC%2BD38XnvVSrsrY%3D 10.1002/cncr.10823 12216092 (Pubitemid 35013059)
    • (2002) Cancer , vol.95 , Issue.6 , pp. 1247-1257
    • Rao, J.Y.1    Seligson, D.2    Visapaa, H.3    Horvath, S.4    Eeva, M.5    Michel, K.6    Pantuck, A.7    Belldegrun, A.8    Palotie, A.9
  • 26
    • 0033593346 scopus 로고    scopus 로고
    • Selected subunits of the cytosolic chaperonin associate with microtubules assembled in vitro
    • DOI 10.1074/jbc.274.4.2408
    • A Roobol ZP Sahyoun MJ Carden 1999 Selected subunits of the cytosolic chaperonin associate with microtubules assembled in vitro J Biol Chem 274 2408 2415 1:CAS:528:DyaK1MXovVGrtg%3D%3D 10.1074/jbc.274.4.2408 9891010 (Pubitemid 29061402)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.4 , pp. 2408-2415
    • Roobol, A.1    Sahyoun, Z.P.2    Carden, M.J.3
  • 30
    • 57149098022 scopus 로고    scopus 로고
    • Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
    • 1:CAS:528:DC%2BD1cXhsVWhu7bK 10.1038/nsmb.1515
    • AY Yam Y Xia H-TJ Lin A Burlingame M Gerstein J Frydman 2008 Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies J Nat Struct Mol Biol 15 1255 1262 1:CAS:528:DC%2BD1cXhsVWhu7bK 10.1038/nsmb.1515
    • (2008) J Nat Struct Mol Biol , vol.15 , pp. 1255-1262
    • Yam, A.Y.1    Xia, Y.2    H-Tj, L.3    Burlingame, A.4    Gerstein, M.5    Frydman, J.6


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