메뉴 건너뛰기




Volumn 312, Issue 2, 2006, Pages 198-204

Intracellular dynamics of the Hsp90 co-chaperone p23 is dictated by Hsp90

Author keywords

Confocal microscopy; In vivo; Interaction; Kinetics; Molecular chaperone

Indexed keywords

CELL CYCLE PROTEIN 23; GELDANAMYCIN; GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN 90; HYBRID PROTEIN; PROTEIN P23; UNCLASSIFIED DRUG;

EID: 28344446376     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2005.10.009     Document Type: Article
Times cited : (34)

References (38)
  • 1
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • D. Picard Heat-shock protein 90, a chaperone for folding and regulation Cell. Mol. Life Sci. 59 2002 1640 1648
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 3
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • D.F. Nathan, M.H. Vos, and S. Lindquist In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone Proc. Natl. Acad. Sci. U. S. A. 94 1997 12949 12956
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 5
    • 0028266874 scopus 로고
    • Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes
    • J.L. Johnson, T.G. Beito, C.J. Krco, and D.O. Toft Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes Mol. Cell. Biol. 14 1994 1956 1963
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1956-1963
    • Johnson, J.L.1    Beito, T.G.2    Krco, C.J.3    Toft, D.O.4
  • 6
    • 0042026348 scopus 로고    scopus 로고
    • P23, a simple protein with complex activities
    • S.J. Felts, and D.O. Toft p23, a simple protein with complex activities Cell Stress Chaperones 8 2003 108 113
    • (2003) Cell Stress Chaperones , vol.8 , pp. 108-113
    • Felts, S.J.1    Toft, D.O.2
  • 7
    • 0029872081 scopus 로고    scopus 로고
    • The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes
    • J. Johnson, R. Corbisier, B. Stensgard, and D.O. Toft The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes J. Steroid Biochem. Mol. Biol. 56 1996 31 37
    • (1996) J. Steroid Biochem. Mol. Biol. , vol.56 , pp. 31-37
    • Johnson, J.1    Corbisier, R.2    Stensgard, B.3    Toft, D.O.4
  • 8
    • 0029075280 scopus 로고
    • Binding of p23 and hsp90 during assembly with the progesterone receptor
    • J.L. Johnson, and D.O. Toft Binding of p23 and hsp90 during assembly with the progesterone receptor Mol. Endocrinol. 9 1995 670 678
    • (1995) Mol. Endocrinol. , vol.9 , pp. 670-678
    • Johnson, J.L.1    Toft, D.O.2
  • 9
    • 0034725641 scopus 로고    scopus 로고
    • Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone
    • A.J. Weaver, W.P. Sullivan, S.J. Felts, B.A. Owen, and D.O. Toft Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone J. Biol. Chem. 275 2000 23045 23052
    • (2000) J. Biol. Chem. , vol.275 , pp. 23045-23052
    • Weaver, A.J.1    Sullivan, W.P.2    Felts, S.J.3    Owen, B.A.4    Toft, D.O.5
  • 11
    • 4444291743 scopus 로고    scopus 로고
    • The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle
    • K. Richter, S. Walter, and J. Buchner The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle J. Mol. Biol. 342 2004 1403 1413
    • (2004) J. Mol. Biol. , vol.342 , pp. 1403-1413
    • Richter, K.1    Walter, S.2    Buchner, J.3
  • 13
    • 0037195951 scopus 로고    scopus 로고
    • The influence of ATP and p23 on the conformation of hsp90
    • W.P. Sullivan, B.A. Owen, and D.O. Toft The influence of ATP and p23 on the conformation of hsp90 J. Biol. Chem. 277 2002 45942 45948
    • (2002) J. Biol. Chem. , vol.277 , pp. 45942-45948
    • Sullivan, W.P.1    Owen, B.A.2    Toft, D.O.3
  • 14
    • 0036303385 scopus 로고    scopus 로고
    • Stimulation of the weak ATPase activity of human Hsp90 by a client protein
    • S.H. McLaughlin, H.W. Smith, and S.E. Jackson Stimulation of the weak ATPase activity of human Hsp90 by a client protein J. Mol. Biol. 315 2002 787 798
    • (2002) J. Mol. Biol. , vol.315 , pp. 787-798
    • McLaughlin, S.H.1    Smith, H.W.2    Jackson, S.E.3
  • 15
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • W.B. Pratt, and D.O. Toft Steroid receptor interactions with heat shock protein and immunophilin chaperones Endocr. Rev. 18 1997 306 360
    • (1997) Endocr. Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 16
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
    • M.G. Marcu, A. Chadli, I. Bouhouche, M. Catelli, and L.M. Neckers The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone J. Biol. Chem. 275 2000 37181 37186
    • (2000) J. Biol. Chem. , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 18
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • J.S. Isaacs, W. Xu, and L. Neckers Heat shock protein 90 as a molecular target for cancer therapeutics Cancer Cell 3 2003 213 217
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 19
    • 0141596941 scopus 로고    scopus 로고
    • Overview: Translating Hsp90 biology into Hsp90 drugs
    • P. Workman Overview: translating Hsp90 biology into Hsp90 drugs Curr. Cancer Drug Targets 3 2003 297 300
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 297-300
    • Workman, P.1
  • 20
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90-associated proteins
    • S. Bose, T. Weikl, H. Bügl, and J. Buchner Chaperone function of Hsp90-associated proteins Science 274 1996 1715 1717
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Bügl, H.3    Buchner, J.4
  • 21
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cylophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • B.C. Freeman, D.O. Toft, and R.I. Morimoto Molecular chaperone machines: chaperone activities of the cylophilin Cyp-40 and the steroid aporeceptor-associated protein p23 Science 274 1996 1718 1720
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 22
    • 0034102339 scopus 로고    scopus 로고
    • The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
    • B.C. Freeman, S.J. Felts, D.O. Toft, and K.R. Yamamoto The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies Genes Dev. 14 2000 422 434
    • (2000) Genes Dev. , vol.14 , pp. 422-434
    • Freeman, B.C.1    Felts, S.J.2    Toft, D.O.3    Yamamoto, K.R.4
  • 23
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • B.C. Freeman, and K.R. Yamamoto Disassembly of transcriptional regulatory complexes by molecular chaperones Science 296 2002 2232 2235
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 24
    • 0034693050 scopus 로고    scopus 로고
    • Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis
    • T. Tanioka, Y. Nakatani, N. Semmyo, M. Murakami, and I. Kudo Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis J. Biol. Chem. 275 2000 32775 32782
    • (2000) J. Biol. Chem. , vol.275 , pp. 32775-32782
    • Tanioka, T.1    Nakatani, Y.2    Semmyo, N.3    Murakami, M.4    Kudo, I.5
  • 27
    • 13244291467 scopus 로고    scopus 로고
    • FRAP analysis of binding: Proper and fitting
    • B.L. Sprague, and J.G. McNally FRAP analysis of binding: proper and fitting Trends Cell Biol. 15 2005 84 91
    • (2005) Trends Cell Biol. , vol.15 , pp. 84-91
    • Sprague, B.L.1    McNally, J.G.2
  • 28
    • 2942690158 scopus 로고    scopus 로고
    • Analysis of binding reactions by fluorescence recovery after photobleaching
    • B.L. Sprague, R.L. Pego, D.A. Stavreva, and J.G. McNally Analysis of binding reactions by fluorescence recovery after photobleaching Biophys. J. 86 2004 3473 3495
    • (2004) Biophys. J. , vol.86 , pp. 3473-3495
    • Sprague, B.L.1    Pego, R.L.2    Stavreva, D.A.3    McNally, J.G.4
  • 29
    • 22444447736 scopus 로고    scopus 로고
    • Imaging molecular interactions in living cells
    • R.N. Day, and F. Schaufele Imaging molecular interactions in living cells Mol. Endocrinol. 19 2005 1675 1686
    • (2005) Mol. Endocrinol. , vol.19 , pp. 1675-1686
    • Day, R.N.1    Schaufele, F.2
  • 30
    • 1342286829 scopus 로고    scopus 로고
    • Inhibition of GR-mediated transcription by p23 requires interaction with Hsp90
    • G.M. Wochnik, J.C. Young, U. Schmidt, F. Holsboer, F.U. Hartl, and T. Rein Inhibition of GR-mediated transcription by p23 requires interaction with Hsp90 FEBS Lett. 560 2004 35 38
    • (2004) FEBS Lett. , vol.560 , pp. 35-38
    • Wochnik, G.M.1    Young, J.C.2    Schmidt, U.3    Holsboer, F.4    Hartl, F.U.5    Rein, T.6
  • 31
    • 12144290835 scopus 로고    scopus 로고
    • Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes
    • D.A. Stavreva, W.G. Müller, G.L. Hager, C.L. Smith, and J.G. McNally Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes Mol. Cell. Biol. 24 2004 2682 2697
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2682-2697
    • Stavreva, D.A.1    Müller, W.G.2    Hager, G.L.3    Smith, C.L.4    McNally, J.G.5
  • 32
    • 0032760261 scopus 로고    scopus 로고
    • An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function
    • T. Weikl, K. Abelmann, and J. Buchner An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function J. Mol. Biol. 293 1999 685 691
    • (1999) J. Mol. Biol. , vol.293 , pp. 685-691
    • Weikl, T.1    Abelmann, K.2    Buchner, J.3
  • 33
    • 0020568317 scopus 로고
    • Theoretical analysis of fluorescence photobleaching recovery experiments
    • D.M. Soumpasis Theoretical analysis of fluorescence photobleaching recovery experiments Biophys. J. 41 1983 95 97
    • (1983) Biophys. J. , vol.41 , pp. 95-97
    • Soumpasis, D.M.1
  • 34
  • 37
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: Molecular chaperones as stress-sensing 'heat shock' proteins
    • E.A. Nollen, and R.I. Morimoto Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins J. Cell Sci. 115 2002 2809 2816
    • (2002) J. Cell Sci. , vol.115 , pp. 2809-2816
    • Nollen, E.A.1    Morimoto, R.I.2
  • 38
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • R.Y. Tsien The green fluorescent protein Annu. Rev. Biochem. 67 1998 509 544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.