메뉴 건너뛰기




Volumn 15, Issue 3, 2016, Pages 588-598

Systematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 Function

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOCORTICOID RECEPTOR; HEAT SHOCK PROTEIN 90; ADENINE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMINO ACID;

EID: 84962652418     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2016.03.046     Document Type: Article
Times cited : (67)

References (56)
  • 1
    • 0033959642 scopus 로고    scopus 로고
    • The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest
    • Abbas-Terki T., Donzé O., Picard D. The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest. FEBS Lett. 2000, 467:111-116.
    • (2000) FEBS Lett. , vol.467 , pp. 111-116
    • Abbas-Terki, T.1    Donzé, O.2    Picard, D.3
  • 5
    • 0034015979 scopus 로고    scopus 로고
    • A transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in caenorhabditis elegans
    • Birnby D.A., Link E.M., Vowels J.J., Tian H., Colacurcio P.L., Thomas J.H. A transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in caenorhabditis elegans. Genetics 2000, 155:85-104.
    • (2000) Genetics , vol.155 , pp. 85-104
    • Birnby, D.A.1    Link, E.M.2    Vowels, J.J.3    Tian, H.4    Colacurcio, P.L.5    Thomas, J.H.6
  • 7
    • 0024421221 scopus 로고
    • Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich K.A., Farrelly F.W., Finkelstein D.B., Taulien J., Lindquist S. hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell. Biol. 1989, 9:3919-3930.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 9
    • 84905217368 scopus 로고    scopus 로고
    • Deep mutational scanning: a new style of protein science
    • Fowler D.M., Fields S. Deep mutational scanning: a new style of protein science. Nat. Methods 2014, 11:801-807.
    • (2014) Nat. Methods , vol.11 , pp. 801-807
    • Fowler, D.M.1    Fields, S.2
  • 11
    • 2942533020 scopus 로고    scopus 로고
    • The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site
    • Harris S.F., Shiau A.K., Agard D.A. The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 2004, 12:1087-1097.
    • (2004) Structure , vol.12 , pp. 1087-1097
    • Harris, S.F.1    Shiau, A.K.2    Agard, D.A.3
  • 12
    • 33750983940 scopus 로고    scopus 로고
    • The middle domain of Hsp90 acts as a discriminator between different types of client proteins
    • Hawle P., Siepmann M., Harst A., Siderius M., Reusch H.P., Obermann W.M. The middle domain of Hsp90 acts as a discriminator between different types of client proteins. Mol. Cell. Biol. 2006, 26:8385-8395.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8385-8395
    • Hawle, P.1    Siepmann, M.2    Harst, A.3    Siderius, M.4    Reusch, H.P.5    Obermann, W.M.6
  • 14
    • 84866782988 scopus 로고    scopus 로고
    • Fitness analyses of all possible point mutations for regions of genes in yeast
    • Hietpas R., Roscoe B., Jiang L., Bolon D.N. Fitness analyses of all possible point mutations for regions of genes in yeast. Nat. Protoc. 2012, 7:1382-1396.
    • (2012) Nat. Protoc. , vol.7 , pp. 1382-1396
    • Hietpas, R.1    Roscoe, B.2    Jiang, L.3    Bolon, D.N.4
  • 15
    • 84888829471 scopus 로고    scopus 로고
    • Shifting fitness landscapes in response to altered environments
    • Hietpas R.T., Bank C., Jensen J.D., Bolon D.N. Shifting fitness landscapes in response to altered environments. Evolution 2013, 67:3512-3522.
    • (2013) Evolution , vol.67 , pp. 3512-3522
    • Hietpas, R.T.1    Bank, C.2    Jensen, J.D.3    Bolon, D.N.4
  • 16
    • 84879619070 scopus 로고    scopus 로고
    • Latent effects of Hsp90 mutants revealed at reduced expression levels
    • Jiang L., Mishra P., Hietpas R.T., Zeldovich K.B., Bolon D.N. Latent effects of Hsp90 mutants revealed at reduced expression levels. PLoS Genet. 2013, 9:e1003600.
    • (2013) PLoS Genet. , vol.9 , pp. e1003600
    • Jiang, L.1    Mishra, P.2    Hietpas, R.T.3    Zeldovich, K.B.4    Bolon, D.N.5
  • 17
  • 19
    • 84903149823 scopus 로고    scopus 로고
    • Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles
    • Kirschke E., Goswami D., Southworth D., Griffin P.R., Agard D.A. Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles. Cell 2014, 157:1685-1697.
    • (2014) Cell , vol.157 , pp. 1685-1697
    • Kirschke, E.1    Goswami, D.2    Southworth, D.3    Griffin, P.R.4    Agard, D.A.5
  • 20
    • 84875225582 scopus 로고    scopus 로고
    • Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle
    • Li J., Richter K., Reinstein J., Buchner J. Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Nat. Struct. Mol. Biol. 2013, 20:326-331.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 326-331
    • Li, J.1    Richter, K.2    Reinstein, J.3    Buchner, J.4
  • 21
    • 0031795189 scopus 로고    scopus 로고
    • Hsp90 is required for pheromone signaling in yeast
    • Louvion J.F., Abbas-Terki T., Picard D. Hsp90 is required for pheromone signaling in yeast. Mol. Biol. Cell 1998, 9:3071-3083.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3071-3083
    • Louvion, J.F.1    Abbas-Terki, T.2    Picard, D.3
  • 22
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions
    • Meyer P., Prodromou C., Hu B., Vaughan C., Roe S.M., Panaretou B., Piper P.W., Pearl L.H. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol. Cell 2003, 11:647-658.
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6    Piper, P.W.7    Pearl, L.H.8
  • 24
    • 84874267225 scopus 로고    scopus 로고
    • The therapeutic target Hsp90 and cancer hallmarks
    • Miyata Y., Nakamoto H., Neckers L. The therapeutic target Hsp90 and cancer hallmarks. Curr. Pharm. Des. 2013, 19:347-365.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 347-365
    • Miyata, Y.1    Nakamoto, H.2    Neckers, L.3
  • 25
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase
    • Nathan D.F., Lindquist S. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol Cell Biol 1995, 15:3917-3925.
    • (1995) Mol Cell Biol , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 26
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • Nathan D.F., Vos M.H., Lindquist S. In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc. Natl. Acad. Sci. USA 1997, 94:12949-12956.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 27
    • 84892746838 scopus 로고    scopus 로고
    • Stressing the development of small molecules targeting HSP90
    • Neckers L., Trepel J.B. Stressing the development of small molecules targeting HSP90. Clin. Cancer Res. 2014, 20:275-277.
    • (2014) Clin. Cancer Res. , vol.20 , pp. 275-277
    • Neckers, L.1    Trepel, J.B.2
  • 28
    • 0023809599 scopus 로고
    • Coupled assay of Na+,K+-ATPase activity
    • Nørby J.G. Coupled assay of Na+,K+-ATPase activity. Methods Enzymol. 1988, 156:116-119.
    • (1988) Methods Enzymol. , vol.156 , pp. 116-119
    • Nørby, J.G.1
  • 30
    • 0015722319 scopus 로고
    • Slightly deleterious mutant substitutions in evolution
    • Ohta T. Slightly deleterious mutant substitutions in evolution. Nature 1973, 246:96-98.
    • (1973) Nature , vol.246 , pp. 96-98
    • Ohta, T.1
  • 31
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou B., Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 1998, 17:4829-4836.
    • (1998) EMBO J. , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 34
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 1997, 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
  • 36
    • 79953202216 scopus 로고    scopus 로고
    • Enforced N-domain proximity stimulates Hsp90 ATPase activity and is compatible with function in vivo
    • Pullen L., Bolon D.N. Enforced N-domain proximity stimulates Hsp90 ATPase activity and is compatible with function in vivo. J. Biol. Chem. 2011, 286:11091-11098.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11091-11098
    • Pullen, L.1    Bolon, D.N.2
  • 37
    • 84865619780 scopus 로고    scopus 로고
    • Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth
    • Pursell N.W., Mishra P., Bolon D.N. Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth. Eukaryot. Cell 2012, 11:1033-1041.
    • (2012) Eukaryot. Cell , vol.11 , pp. 1033-1041
    • Pursell, N.W.1    Mishra, P.2    Bolon, D.N.3
  • 38
    • 84903216307 scopus 로고    scopus 로고
    • Four-colour FRET reveals directionality in the Hsp90 multicomponent machinery
    • Ratzke C., Hellenkamp B., Hugel T. Four-colour FRET reveals directionality in the Hsp90 multicomponent machinery. Nat. Commun. 2014, 5:4192.
    • (2014) Nat. Commun. , vol.5 , pp. 4192
    • Ratzke, C.1    Hellenkamp, B.2    Hugel, T.3
  • 43
    • 33750008686 scopus 로고    scopus 로고
    • Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
    • Shiau A.K., Harris S.F., Southworth D.R., Agard D.A. Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 2006, 127:329-340.
    • (2006) Cell , vol.127 , pp. 329-340
    • Shiau, A.K.1    Harris, S.F.2    Southworth, D.R.3    Agard, D.A.4
  • 44
    • 56849131626 scopus 로고    scopus 로고
    • Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle
    • Southworth D.R., Agard D.A. Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle. Mol. Cell 2008, 32:631-640.
    • (2008) Mol. Cell , vol.32 , pp. 631-640
    • Southworth, D.R.1    Agard, D.A.2
  • 45
    • 0025808091 scopus 로고
    • Proline for alanine substitutions in the C-peptide helix of ribonuclease A
    • Strehlow K.G., Robertson A.D., Baldwin R.L. Proline for alanine substitutions in the C-peptide helix of ribonuclease A. Biochemistry 1991, 30:5810-5814.
    • (1991) Biochemistry , vol.30 , pp. 5810-5814
    • Strehlow, K.G.1    Robertson, A.D.2    Baldwin, R.L.3
  • 46
    • 84865695733 scopus 로고    scopus 로고
    • Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition
    • Taipale M., Krykbaeva I., Koeva M., Kayatekin C., Westover K.D., Karras G.I., Lindquist S. Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. Cell 2012, 150:987-1001.
    • (2012) Cell , vol.150 , pp. 987-1001
    • Taipale, M.1    Krykbaeva, I.2    Koeva, M.3    Kayatekin, C.4    Westover, K.D.5    Karras, G.I.6    Lindquist, S.7
  • 47
  • 48
    • 0023376280 scopus 로고
    • Two genes required for cell fusion during yeast conjugation: evidence for a pheromone-induced surface protein
    • Trueheart J., Boeke J.D., Fink G.R. Two genes required for cell fusion during yeast conjugation: evidence for a pheromone-induced surface protein. Mol. Cell. Biol. 1987, 7:2316-2328.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2316-2328
    • Trueheart, J.1    Boeke, J.D.2    Fink, G.R.3
  • 49
    • 42449128411 scopus 로고    scopus 로고
    • Population genomics of the wild yeast Saccharomyces paradoxus: Quantifying the life cycle
    • Tsai I.J., Bensasson D., Burt A., Koufopanou V. Population genomics of the wild yeast Saccharomyces paradoxus: Quantifying the life cycle. Proc. Natl. Acad. Sci. USA 2008, 105:4957-4962.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4957-4962
    • Tsai, I.J.1    Bensasson, D.2    Burt, A.3    Koufopanou, V.4
  • 51
    • 36849083947 scopus 로고    scopus 로고
    • Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers
    • Wayne N., Bolon D.N. Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers. J. Biol. Chem. 2007, 282:35386-35395.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35386-35395
    • Wayne, N.1    Bolon, D.N.2
  • 52
    • 73649144525 scopus 로고    scopus 로고
    • Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo
    • Wayne N., Lai Y., Pullen L., Bolon D.N. Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo. J. Biol. Chem. 2010, 285:234-241.
    • (2010) J. Biol. Chem. , vol.285 , pp. 234-241
    • Wayne, N.1    Lai, Y.2    Pullen, L.3    Bolon, D.N.4
  • 54
    • 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., Mimnaugh E.G., De Costa B., Myers C.E., Neckers L.M. 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 1994, 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
  • 55
    • 0027291238 scopus 로고
    • Heat-shock protein hsp90 governs the activity of pp60v-src kinase
    • Xu Y., Lindquist S. Heat-shock protein hsp90 governs the activity of pp60v-src kinase. Proc. Natl. Acad. Sci. USA 1993, 90:7074-7078.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7074-7078
    • Xu, Y.1    Lindquist, S.2
  • 56
    • 0033524442 scopus 로고    scopus 로고
    • Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90
    • Xu Y., Singer M.A., Lindquist S. Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90. Proc. Natl. Acad. Sci. USA 1999, 96:109-114.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 109-114
    • Xu, Y.1    Singer, M.A.2    Lindquist, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.