메뉴 건너뛰기




Volumn 17, Issue 2, 1997, Pages 594-603

Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOSPORIN; GENE PRODUCT; IMMUNOPHILIN; PROGESTERONE RECEPTOR;

EID: 0031053574     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.2.594     Document Type: Article
Times cited : (173)

References (46)
  • 2
    • 0022574582 scopus 로고
    • src with the cellular proteins pp50 and pp90
    • src with the cellular proteins pp50 and pp90. Curr. Top. Microbiol. Immunol. 12:1-22
    • (1986) Curr. Top. Microbiol. Immunol. , vol.12 , pp. 1-22
    • Brugge, J.1
  • 3
    • 0029885423 scopus 로고    scopus 로고
    • Interactions of p60, a mediator of progesterone receptor assembly, with Hsp90 and Hsp70
    • Chen, S., V. Prapapanich, R. A. Rimerman, R. Honoré, and D. F. Smith. 1996. Interactions of p60, a mediator of progesterone receptor assembly, with Hsp90 and Hsp70. Mol. Endocrinol. 10:682-693.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 682-693
    • Chen, S.1    Prapapanich, V.2    Rimerman, R.A.3    Honoré, R.4    Smith, D.F.5
  • 5
    • 0025922586 scopus 로고
    • The TPR snap helix: A novel protein repeat from mitosis to transcription
    • Goebl, M., and M. Yanagida. 1991. The TPR snap helix: a novel protein repeat from mitosis to transcription. Trends Biochem. Sci. 16:173-177.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 173-177
    • Goebl, M.1    Yanagida, M.2
  • 6
    • 0028842615 scopus 로고
    • Hip, a new cochaperone involved in the eukaryotic hsc70/Hsp40 reaction cycle
    • Höhfeld, J., Y. Minami, and F.-U. Hartl. 1995. Hip, a new cochaperone involved in the eukaryotic hsc70/Hsp40 reaction cycle. Cell 83:589-598.
    • (1995) Cell , vol.83 , pp. 589-598
    • Höhfeld, J.1    Minami, Y.2    Hartl, F.-U.3
  • 7
    • 0026640657 scopus 로고
    • Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1
    • Honoré, B., H. Leffers, P. Madsen, H. H. Rasmussen, J. Vandekerckhove, and J. E. Celis. 1992. Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1. J. Biol. Chem. 267:8485-8491.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8485-8491
    • Honoré, B.1    Leffers, H.2    Madsen, P.3    Rasmussen, H.H.4    Vandekerckhove, J.5    Celis, J.E.6
  • 9
    • 0028266874 scopus 로고
    • Characterization of a novel 23-kDa protein of unactive progesterone receptor complexes
    • Johnson, J. L., T. G. Beito, C. J. Kreo, and D. O. Toft. 1994. Characterization of a novel 23-kDa protein of unactive progesterone receptor complexes. Mol. Cell. Biol. 14:1956-1963.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1956-1963
    • Johnson, J.L.1    Beito, T.G.2    Kreo, C.J.3    Toft, D.O.4
  • 10
    • 0029872081 scopus 로고    scopus 로고
    • The involvement of p23. Hsp90. and immunophilins in the assembly of progesterone receptor complexes
    • Johnson, J. L., R. Corbisier, B. Stensgard, and D. Toft. 1996. The involvement of p23. Hsp90. and immunophilins in the assembly of progesterone receptor complexes. J. Steroid Biochem. Mol. Biol. 56:31-37.
    • (1996) J. Steroid Biochem. Mol. Biol. , vol.56 , pp. 31-37
    • Johnson, J.L.1    Corbisier, R.2    Stensgard, B.3    Toft, D.4
  • 11
    • 0028027504 scopus 로고
    • A novel chaperone complex for steroid receptors involving heat shock protein, immunophilins and p23
    • Johnson, J. L., and D. O. Toft. 1994. A novel chaperone complex for steroid receptors involving heat shock protein, immunophilins and p23. J. Biol. Chem. 269:24989-24993.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24989-24993
    • Johnson, J.L.1    Toft, D.O.2
  • 12
    • 0029075280 scopus 로고
    • Binding of p23 and Hsp90 during assembly with the progesterone receptor
    • Johnson, J. L., and D. O. Toft. 1995. Binding of p23 and Hsp90 during assembly with the progesterone receptor. Mol. Endocrinol. 9:670-678.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 670-678
    • Johnson, J.L.1    Toft, D.O.2
  • 13
    • 0029867394 scopus 로고    scopus 로고
    • Structure-function relationships in the FK506-binding protein (FKBP) family of peptidylprolyl cis-trans isomerases
    • Kay, J. E. 1996. Structure-function relationships in the FK506-binding protein (FKBP) family of peptidylprolyl cis-trans isomerases. Biochem. J. 314: 361-385.
    • (1996) Biochem. J. , vol.314 , pp. 361-385
    • Kay, J.E.1
  • 14
    • 0027217548 scopus 로고
    • Cyclophilin-40, a protein with homology to the p59 component of the steroid receptor complex: Cloning of the cDNA and further characterization
    • Kieffer, L. J., T. W. Seng, W. Li, D. G. Osterman, R. E. Handschumacher, and R. M. Bayney. 1993. Cyclophilin-40, a protein with homology to the p59 component of the steroid receptor complex: cloning of the cDNA and further characterization. J. Biol. Chem. 268:12303-12310.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12303-12310
    • Kieffer, L.J.1    Seng, T.W.2    Li, W.3    Osterman, D.G.4    Handschumacher, R.E.5    Bayney, R.M.6
  • 15
    • 0030035694 scopus 로고    scopus 로고
    • An FK506-sensitive transporter selectively decreases intracellular levels and potency of steroid hormones
    • Kralli, A., and K. R. Yamamoto. 1996. An FK506-sensitive transporter selectively decreases intracellular levels and potency of steroid hormones. J. Biol. Chem. 271:17152-17156.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17152-17156
    • Kralli, A.1    Yamamoto, K.R.2
  • 19
    • 84920295385 scopus 로고    scopus 로고
    • A pathway of multi-chaperone interactions common to diverse regulatory proteins: Estrogen receptor, Fes tyrosine kinase, heat shock transcription factor HSF1, and the arylhydrocarbon receptor
    • in press
    • Nair, S. C., E. J. Toran, R. A. Rimerman, S. Hjermstad, T. E. Smithgall, and D. F. Smith. A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor HSF1, and the arylhydrocarbon receptor. Cell Stress Chap., in press.
    • Cell Stress Chap.
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hjermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 20
    • 0029101382 scopus 로고
    • The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin Hsp56 hind to a common site on Hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor
    • Owens-Grillo, J. K., K. Hoffman, K. A. Hutchison, A. W. Yem, M. R. Deibel, Jr., R. E. Handschumacher, and W. B. Pratt. 1995. The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin Hsp56 hind to a common site on Hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor. J. Biol. Chem. 270: 20479-20484.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20479-20484
    • Owens-Grillo, J.K.1    Hoffman, K.2    Hutchison, K.A.3    Yem, A.W.4    Deibel Jr., M.R.5    Handschumacher, R.E.6    Pratt, W.B.7
  • 21
    • 0026495863 scopus 로고
    • Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes
    • Peattie, D. A., M. W. Harding, M. A. Fleming, M. T. DeCenzo, J. A. Lippke, D. J. Livingston, and M. Beasutti. 1992. Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes. Proc. Natl. Acad. Sci. USA 89:10974-10978.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10974-10978
    • Peattie, D.A.1    Harding, M.W.2    Fleming, M.A.3    DeCenzo, M.T.4    Lippke, J.A.5    Livingston, D.J.6    Beasutti, M.7
  • 22
    • 0029964506 scopus 로고    scopus 로고
    • 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. 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
  • 24
    • 0027366385 scopus 로고
    • The Hsp56 immunophilin component of steroid receptor heterocomplexes: Could this be the elusive nuclear localization signal-binding protein?
    • Pratt, W. B., M. J. Czar, L. F. Stancato, and J. K. Grillo. 1993. The Hsp56 immunophilin component of steroid receptor heterocomplexes: could this be the elusive nuclear localization signal-binding protein? J. Steroid Biochem. Mol. Biol. 46:269-279.
    • (1993) J. Steroid Biochem. Mol. Biol. , vol.46 , pp. 269-279
    • Pratt, W.B.1    Czar, M.J.2    Stancato, L.F.3    Grillo, J.K.4
  • 25
    • 0027962531 scopus 로고
    • The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain
    • Radanyi, C., B. Chambraud, and E.-E. Baulieu. 1994. The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain. Proc. Natl. Acad. Sci. USA 91:11197-11201.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11197-11201
    • Radanyi, C.1    Chambraud, B.2    Baulieu, E.-E.3
  • 26
    • 0030050335 scopus 로고    scopus 로고
    • Cyclophilin 40 (CyP-40), mapping of its Hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for Hsp90 binding
    • Ratajczak, T., and A. Carrello. 1996. Cyclophilin 40 (CyP-40), mapping of its Hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for Hsp90 binding. J. Biol. Chem. 271:2961-2965.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2961-2965
    • Ratajczak, T.1    Carrello, A.2
  • 27
    • 0027438228 scopus 로고
    • The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59)
    • Ratajczak, T., A. Carrello, P. J. Mark, B. J. Warner, R. J. Simpson, R. L. Moritz, and A. K. House. 1993. The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59). J. Biol. Chem. 268:13187-13192.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13187-13192
    • Ratajczak, T.1    Carrello, A.2    Mark, P.J.3    Warner, B.J.4    Simpson, R.J.5    Moritz, R.L.6    House, A.K.7
  • 28
    • 0025337581 scopus 로고
    • The non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contains a Hsp90-bound 59-kilodalton protein
    • Renoir, J.-M., C. Radanyi, L. E. Faber, and E.-E. Baulieu. 1990. The non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contains a Hsp90-bound 59-kilodalton protein. J. Biol. Chem. 265: 10740-10745.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10740-10745
    • Renoir, J.-M.1    Radanyi, C.2    Faber, L.E.3    Baulieu, E.-E.4
  • 30
    • 0025605444 scopus 로고
    • Hsp56: A novel heat shock protein associated with untranstormed steroid receptor complexes
    • Sanchez, E. R. 1990. Hsp56: a novel heat shock protein associated with untranstormed steroid receptor complexes. J. Biol. Chem. 265:22067-22070.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22067-22070
    • Sanchez, E.R.1
  • 31
    • 0025290187 scopus 로고
    • The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70-and 90-kilodalton heat shock proteins
    • Sanchez, E. R., L. E. Faber, W. J. Henzel, and W. B. Pratt. 1990. The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70-and 90-kilodalton heat shock proteins. Biochemistry 29:5145-5152.
    • (1990) Biochemistry , vol.29 , pp. 5145-5152
    • Sanchez, E.R.1    Faber, L.E.2    Henzel, W.J.3    Pratt, W.B.4
  • 32
    • 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
  • 33
    • 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
  • 34
    • 85035189515 scopus 로고    scopus 로고
    • Unpublished data
    • Smith, D. F. Unpublished data.
    • Smith, D.F.1
  • 35
    • 0027361272 scopus 로고
    • FKBP54, a novel FK506-binding protein in avian progesterone receptor complexes and HeLa extracts
    • Smith, D. F., M. W. Albers, S. L. Schreiber, K. L. Leach, and M. R. Deibel. 1993. FKBP54, a novel FK506-binding protein in avian progesterone receptor complexes and HeLa extracts. J. Biol. Chem. 268:24270-24273.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24270-24273
    • Smith, D.F.1    Albers, M.W.2    Schreiber, S.L.3    Leach, K.L.4    Deibel, M.R.5
  • 36
    • 0027219348 scopus 로고
    • Two FKBP-related proteins are components of progesterone receptor complexes
    • Smith, D. F., B. A. Baggenstoss, T. N. Marion, and R. A. Rimerman. 1993. Two FKBP-related proteins are components of progesterone receptor complexes. J. Biol. Chem. 268:18365-18371.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18365-18371
    • Smith, D.F.1    Baggenstoss, B.A.2    Marion, T.N.3    Rimerman, R.A.4
  • 37
    • 0025233648 scopus 로고
    • Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins
    • Smith, D. F., L. E. Faber, and D. O. Toft. 1990. Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins. J. Biol. Chem. 265:3996-4003.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3996-4003
    • Smith, D.F.1    Faber, L.E.2    Toft, D.O.3
  • 39
    • 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
  • 40
    • 0027433644 scopus 로고
    • Raf exists in a native heterocomplex with Hsp90 and p50 that can be reconstituted in a cell-free system
    • Stancato, L. F., Y.-H. Chow, K. A. Hutchison, G. H. Perdew, R. Jove, and W. B. Pratt. 1993. Raf exists in a native heterocomplex with Hsp90 and p50 that can be reconstituted in a cell-free system. J. Biol. Chem. 268:21711-21716.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21711-21716
    • Stancato, L.F.1    Chow, Y.-H.2    Hutchison, K.A.3    Perdew, G.H.4    Jove, R.5    Pratt, W.B.6
  • 41
    • 0001920056 scopus 로고
    • Using DNA fragments as probes
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), John Wiley & Sons, New York, N.Y.
    • Strauss, W. M. 1993. Using DNA fragments as probes. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology. John Wiley & Sons, New York, N.Y.
    • (1993) Current Protocols in Molecular Biology
    • Strauss, W.M.1
  • 42
    • 0026710278 scopus 로고
    • Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex
    • Tai, P.-K. K., M. W. Albers, H. Chang, L. E. Faber, and S. L. Schreiber. 1992. Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex. Science 256:1315-1318.
    • (1992) Science , vol.256 , pp. 1315-1318
    • Tai, P.-K.K.1    Albers, M.W.2    Chang, H.3    Faber, L.E.4    Schreiber, S.L.5
  • 43
    • 0022918191 scopus 로고
    • A 59-kilodalton protein associated with progestin, estrogen, androgen, and glucocorticoid receptors
    • Tai, P.-K. K., Y. Maeda, K. Nakao, N. G. Wakim, J. L. Duhring, and L. E. Faber. 1986. A 59-kilodalton protein associated with progestin, estrogen, androgen, and glucocorticoid receptors. Biochemistry 25:5269-5275.
    • (1986) Biochemistry , vol.25 , pp. 5269-5275
    • Tai, P.-K.K.1    Maeda, Y.2    Nakao, K.3    Wakim, N.G.4    Duhring, J.L.5    Faber, L.E.6
  • 45
    • 0028828951 scopus 로고
    • Identification and characterization of an immunophilin expressed during the clonal expansion phase of adipocyte differentiation
    • Yeh, W.-C., T.-K. Li, B. E. Bierer, and S. L. McKnight. 1995. Identification and characterization of an immunophilin expressed during the clonal expansion phase of adipocyte differentiation. Proc. Natl. Acad. Sci. USA 92:11081-11085.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11081-11085
    • Yeh, W.-C.1    Li, T.-K.2    Bierer, B.E.3    McKnight, S.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.