메뉴 건너뛰기




Volumn 18, Issue 2, 1998, Pages 944-952

Mutation of Hip's carboxy-terminal region inhibits a transitional stage of progesterone receptor assembly

Author keywords

[No Author keywords available]

Indexed keywords

PROGESTERONE RECEPTOR;

EID: 0031931061     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.2.944     Document Type: Article
Times cited : (50)

References (31)
  • 2
    • 0029037015 scopus 로고
    • Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication
    • Buchberger, A., H. Theyssen, H. Schroder, J. S. McCarty, G. Virgallita, P. Milkereit, J. Reinstein, and B. Bukau. 1995. Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J. Biol. Chem. 270:16903-16910.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16903-16910
    • Buchberger, A.1    Theyssen, H.2    Schroder, H.3    McCarty, J.S.4    Virgallita, G.5    Milkereit, P.6    Reinstein, J.7    Bukau, B.8
  • 3
    • 0031013723 scopus 로고    scopus 로고
    • In vivo analysis of the Hsp90 cochaperone Stil (p60)
    • Chang, H. C., D. F. Nathan, and S. Lindquist. 1997. In vivo analysis of the Hsp90 cochaperone Stil (p60). Mol. Cell. Biol. 17:318-325.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 318-325
    • Chang, H.C.1    Nathan, D.F.2    Lindquist, S.3
  • 4
    • 0029885423 scopus 로고    scopus 로고
    • Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70
    • Chen, S., V. Prapapanich, R. Rimerman, B. Honore, and D. Smith. 1996. Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70. Mol. Endocrinol. 10:682-693.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 682-693
    • Chen, S.1    Prapapanich, V.2    Rimerman, R.3    Honore, B.4    Smith, D.5
  • 5
    • 85036677336 scopus 로고    scopus 로고
    • Chen, S., V. Prapapanich, and D. F. Smith. Unpublished data
    • 4a. Chen, S., V. Prapapanich, and D. F. Smith. Unpublished data.
  • 6
    • 85036685425 scopus 로고    scopus 로고
    • Chen, S., and D. F. Smith. Unpublished results
    • 4b. Chen, S., and D. F. Smith. Unpublished results.
  • 7
    • 17544384391 scopus 로고    scopus 로고
    • Reconstitution of the steroid receptor-hsp90 heterocomplex assembly system of rabbit reticulocyte lysate
    • Dittmar, K. D., K. A. Hutchison, J. K. Owens-Grillo, and W. B. Pratt. 1996. Reconstitution of the steroid receptor-hsp90 heterocomplex assembly system of rabbit reticulocyte lysate. J. Biol. Chem. 271:12833-12839.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12833-12839
    • Dittmar, K.D.1    Hutchison, K.A.2    Owens-Grillo, J.K.3    Pratt, W.B.4
  • 8
    • 0030989277 scopus 로고    scopus 로고
    • Folding of the glucocorticoid receptor by the reconstituted hsp90-based chaperone machinery
    • Dittmar, K. D., and W. B. Pratt. 1997. Folding of the glucocorticoid receptor by the reconstituted hsp90-based chaperone machinery. J. Biol. Chem. 272: 13047-13054.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13047-13054
    • Dittmar, K.D.1    Pratt, W.B.2
  • 9
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • Freeman, B., M. Myers, R. Schumacher, and R. Morimoto. 1995. Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J. 14:2281-2292.
    • (1995) EMBO J. , vol.14 , pp. 2281-2292
    • Freeman, B.1    Myers, M.2    Schumacher, R.3    Morimoto, R.4
  • 10
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman, J., and J. Hohfeld. 1997. Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci. 22:87-92.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Hohfeld, J.2
  • 11
    • 0029787852 scopus 로고    scopus 로고
    • Conformations of the nucleotide and polypeptide binding domains of a cytosolic Hsp70 molecular chaperone are coupled
    • Fung, K. L., L. Hilgenberg, N. M. Wang, and W. J. Chirico. 1996. Conformations of the nucleotide and polypeptide binding domains of a cytosolic Hsp70 molecular chaperone are coupled. J. Biol. Chem. 271:21559-21565.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21559-21565
    • Fung, K.L.1    Hilgenberg, L.2    Wang, N.M.3    Chirico, W.J.4
  • 13
    • 0029927148 scopus 로고    scopus 로고
    • Purification and characterization of a 66-kDa protein from rabbit reticulocyte lysate which promotes the recycling of hsp 70
    • Gross, M., and S. Hessefort. 1996. Purification and characterization of a 66-kDa protein from rabbit reticulocyte lysate which promotes the recycling of hsp 70. J. Biol. Chem. 271:16833-16841.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16833-16841
    • Gross, M.1    Hessefort, S.2
  • 14
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Hoehfeld, J., Y. Minami, and F. U. Hartl. 1995. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83:589-598.
    • (1995) Cell , vol.83 , pp. 589-598
    • Hoehfeld, J.1    Minami, Y.2    Hartl, F.U.3
  • 15
    • 0029161506 scopus 로고
    • The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90
    • Hutchison, K., L. Stancato, J. Owens-Grillo, J. Johnson, P. Krishna, D. Toft, and W. Pratt. 1995. The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90. J. Biol. Chem. 270:18841-18847.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18841-18847
    • Hutchison, K.1    Stancato, L.2    Owens-Grillo, J.3    Johnson, J.4    Krishna, P.5    Toft, D.6    Pratt, W.7
  • 16
    • 0027969323 scopus 로고
    • Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90
    • Hutchison, K. A., K. D. Dittmar, M. J. Czar, and W. B. Pratt. 1993. Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90. J. Biol. Chem. 269:5043-5049.
    • (1993) J. Biol. Chem. , vol.269 , pp. 5043-5049
    • Hutchison, K.A.1    Dittmar, K.D.2    Czar, M.J.3    Pratt, W.B.4
  • 17
    • 0031029286 scopus 로고    scopus 로고
    • Characterization of functional domains of the eukaryotic co-chaperone Hip
    • Irmer, H., and J. Hoehfeld. 1997. Characterization of functional domains of the eukaryotic co-chaperone Hip. J. Biol. Chem. 272:2230-2235.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2230-2235
    • Irmer, H.1    Hoehfeld, J.2
  • 18
    • 0028266874 scopus 로고
    • Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes
    • Johnson, J., T. Beito, C. Krco, and D. Toft. 1994. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol. Cell. Biol. 14:1956-1963.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1956-1963
    • Johnson, J.1    Beito, T.2    Krco, C.3    Toft, D.4
  • 19
    • 0031036746 scopus 로고    scopus 로고
    • Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases
    • Lassle, M., G. L. Blatch, V. Kundra, T. Takatori, and B. R. Zetter. 1997. Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases. J. Biol. Chem. 272:1876-1884.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1876-1884
    • Lassle, M.1    Blatch, G.L.2    Kundra, V.3    Takatori, T.4    Zetter, B.R.5
  • 20
    • 0030018744 scopus 로고    scopus 로고
    • Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis
    • O'Brien, M. C., K. M. Flaherty, and D. B. McKay. 1996. Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis. J. Biol. Chem. 271:15874-15878.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15874-15878
    • O'Brien, M.C.1    Flaherty, K.M.2    McKay, D.B.3
  • 21
    • 0029964506 scopus 로고    scopus 로고
    • Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein
    • Prapapanich, V., S. Chen, S. C. Nair, R. A. Rimerman, and D. F. Smith. 1996. Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein. Mol. Endocrinol. 10:420-431.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 420-431
    • Prapapanich, V.1    Chen, S.2    Nair, S.C.3    Rimerman, R.A.4    Smith, D.F.5
  • 23
    • 85036685339 scopus 로고    scopus 로고
    • Prapapanich, V., and D. F. Smith. Unpublished results
    • Prapapanich, V., and D. F. Smith. Unpublished results.
  • 24
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt, W. B., and D. O. Toft. 1997. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocrine Rev. 18:306-360.
    • (1997) Endocrine Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 25
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C., S. M. Roe, R. O'Brien, J. E. Ladbury, P. W. Piper, and L. H. Pearl. 1997. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90:65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 26
    • 0020445435 scopus 로고
    • A one-step purification of membrane proteins using a high efficiency immunomatrix
    • Schneider, C., R. A. Newman, D. R. Sutherland, U. Asser, and M. F. Greaves. 1982. A one-step purification of membrane proteins using a high efficiency immunomatrix. J. Biol. Chem. 257:10766-10769.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10766-10769
    • Schneider, C.1    Newman, R.A.2    Sutherland, D.R.3    Asser, U.4    Greaves, M.F.5
  • 27
    • 0027439595 scopus 로고
    • Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70
    • Smith, D., W. Sullivan, T. Marion, K. Zaitsu, B. Madden, D. McCormick, and D. Toft. 1993. Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol. Cell. Biol. 13:869-876.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 869-876
    • Smith, D.1    Sullivan, W.2    Marion, T.3    Zaitsu, K.4    Madden, B.5    McCormick, D.6    Toft, D.7
  • 28
    • 0027484097 scopus 로고
    • Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes
    • Smith, D. F. 1993. Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol. Endocrinol. 7:1418-1429.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 1418-1429
    • Smith, D.F.1
  • 29
    • 0026543821 scopus 로고
    • Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events
    • Smith, D. F., B. A. Stensgard, W. J. Welch, and D. O. Toft. 1992. Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events. J. Biol. Chem. 267:1350-1356.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1350-1356
    • Smith, D.F.1    Stensgard, B.A.2    Welch, W.J.3    Toft, D.O.4
  • 30
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an Hsp90-binding agent
    • Smith, D. F., L. Whitesell, S. C. Nair, S. Chen, V. Prapapanich, and R. A. Rimerman. 1995. Progesterone receptor structure and function altered by geldanamycin, an Hsp90-binding agent. Mol. Cell. Biol. 15:6804-6812.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6804-6812
    • Smith, D.F.1    Whitesell, L.2    Nair, S.C.3    Chen, S.4    Prapapanich, V.5    Rimerman, R.A.6
  • 31
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein Hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell, L., E. G. Mimnaugh, B. De Costa, C. E. Myers, and L. M. Neckers. 1994. Inhibition of heat shock protein Hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl. Acad. Sci. USA 91:8324-8328.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.