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Volumn 1823, Issue 3, 2012, Pages 674-682

The role of Hsp90 in protein complex assembly

Author keywords

Complex assembly; Hsp90; Phosphatidylinositol 3 kinase related protein kinase; RNA polymerase II; SnoRNP; Telomere complex

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; EXONUCLEASE; HEAT SHOCK PROTEIN 90; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEASOME; RNA HELICASE; RNA INDUCED SILENCING COMPLEX; RNA POLYMERASE II; SMALL NUCLEOLAR RIBONUCLEOPROTEIN;

EID: 84857053558     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2011.09.001     Document Type: Review
Times cited : (143)

References (109)
  • 2
    • 67650337568 scopus 로고    scopus 로고
    • The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states
    • DeZwaan D.C., Toogun O.A., Echtenkamp F.J., Freeman B.C. The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states. Nat. Struct. Mol. Biol. 2009, 16:711-716.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 711-716
    • DeZwaan, D.C.1    Toogun, O.A.2    Echtenkamp, F.J.3    Freeman, B.C.4
  • 6
    • 77955478739 scopus 로고    scopus 로고
    • Hsc70/Hsp90 chaperone machinery mediates ATP-dependent RISC loading of small RNA duplexes
    • Iwasaki S., Kobayashi M., Yoda M., Sakaguchi Y., Katsuma S., Suzuki T., Tomari Y. Hsc70/Hsp90 chaperone machinery mediates ATP-dependent RISC loading of small RNA duplexes. Mol. Cell 2010, 39:292-299.
    • (2010) Mol. Cell , vol.39 , pp. 292-299
    • Iwasaki, S.1    Kobayashi, M.2    Yoda, M.3    Sakaguchi, Y.4    Katsuma, S.5    Suzuki, T.6    Tomari, Y.7
  • 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
  • 8
    • 0028363670 scopus 로고
    • Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila
    • Cutforth T., Rubin G.M. Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell 1994, 77:1027-1036.
    • (1994) Cell , vol.77 , pp. 1027-1036
    • Cutforth, T.1    Rubin, G.M.2
  • 10
    • 18944365231 scopus 로고    scopus 로고
    • A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p)
    • Millson S.H., Truman A.W., King V., Prodromou C., Pearl L.H., Piper P.W. A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p). Eukaryot. Cell 2005, 4:849-860.
    • (2005) Eukaryot. Cell , vol.4 , pp. 849-860
    • Millson, S.H.1    Truman, A.W.2    King, V.3    Prodromou, C.4    Pearl, L.H.5    Piper, P.W.6
  • 12
    • 34848926209 scopus 로고    scopus 로고
    • Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches
    • McClellan A.J., Xia Y., Deutschbauer A.M., Davis R.W., Gerstein M., Frydman J. Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell 2007, 131:121-135.
    • (2007) Cell , vol.131 , pp. 121-135
    • McClellan, A.J.1    Xia, Y.2    Deutschbauer, A.M.3    Davis, R.W.4    Gerstein, M.5    Frydman, J.6
  • 13
    • 7344241532 scopus 로고    scopus 로고
    • Brassica napus hsp90 can autophosphorylate and phosphorylate other protein substrates
    • Park M., Yong Kang C., Krishna P. Brassica napus hsp90 can autophosphorylate and phosphorylate other protein substrates. Mol. Cell. Biochem. 1998, 185:33-38.
    • (1998) Mol. Cell. Biochem. , vol.185 , pp. 33-38
    • Park, M.1    Yong Kang, C.2    Krishna, P.3
  • 14
    • 69249130057 scopus 로고    scopus 로고
    • The charged linker region is an important regulator of Hsp90 function
    • Hainzl O., Lapina M.C., Buchner J., Richter K. The charged linker region is an important regulator of Hsp90 function. J. Biol. Chem. 2009, 284:22559-22567.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22559-22567
    • Hainzl, O.1    Lapina, M.C.2    Buchner, J.3    Richter, K.4
  • 16
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: emerging mechanistic insights
    • Taipale M., Jarosz D.F., Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell Biol. 2010, 11:515-528.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 17
    • 0033593528 scopus 로고    scopus 로고
    • Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies
    • Maruya M., Sameshima M., Nemoto T., Yahara I. Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies. J. Mol. Biol. 1999, 285:903-907.
    • (1999) J. Mol. Biol. , vol.285 , pp. 903-907
    • Maruya, M.1    Sameshima, M.2    Nemoto, T.3    Yahara, I.4
  • 20
    • 37249011744 scopus 로고    scopus 로고
    • The ATPase cycle of the endoplasmic chaperone Grp94
    • Frey S., Leskovar A., Reinstein J., Buchner J. The ATPase cycle of the endoplasmic chaperone Grp94. J. Biol. Chem. 2007, 282:35612-35620.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35612-35620
    • Frey, S.1    Leskovar, A.2    Reinstein, J.3    Buchner, J.4
  • 22
    • 11344280957 scopus 로고    scopus 로고
    • Extracellular roles for the molecular chaperone, hsp90
    • Eustace B.K., Jay D.G. Extracellular roles for the molecular chaperone, hsp90. Cell Cycle 2004, 3:1098-1100.
    • (2004) Cell Cycle , vol.3 , pp. 1098-1100
    • Eustace, B.K.1    Jay, D.G.2
  • 23
    • 45849149632 scopus 로고    scopus 로고
    • Extracellular HSP90: conquering the cell surface
    • Sidera K., Patsavoudi E. Extracellular HSP90: conquering the cell surface. Cell Cycle 2008, 7:1564-1568.
    • (2008) Cell Cycle , vol.7 , pp. 1564-1568
    • Sidera, K.1    Patsavoudi, E.2
  • 28
    • 43249105354 scopus 로고    scopus 로고
    • P23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity
    • Forafonov F., Toogun O.A., Grad I., Suslova E., Freeman B.C., Picard D. p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity. Mol. Cell. Biol. 2008, 28:3446-3456.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3446-3456
    • Forafonov, F.1    Toogun, O.A.2    Grad, I.3    Suslova, E.4    Freeman, B.C.5    Picard, D.6
  • 32
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
    • Chen S., Smith D.F. Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. J. Biol. Chem. 1998, 273:35194-35200.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 33
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F.U., Moarefi I. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 2000, 101:199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 34
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: a specialized but essential protein-folding tool
    • Young J.C., Moarefi I., Hartl F.U. Hsp90: a specialized but essential protein-folding tool. J. Cell Biol. 2001, 154:267-273.
    • (2001) J. Cell Biol. , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 35
    • 79959344309 scopus 로고    scopus 로고
    • Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:hop complex
    • Southworth D.R., Agard D.A. Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:hop complex. Mol. Cell 2011, 42:771-781.
    • (2011) Mol. Cell , vol.42 , pp. 771-781
    • Southworth, D.R.1    Agard, D.A.2
  • 36
    • 67650681847 scopus 로고    scopus 로고
    • An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell
    • Gong Y., Kakihara Y., Krogan N., Greenblatt J., Emili A., Zhang Z., Houry W.A. An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol. Syst. Biol. 2009, 5:275.
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 275
    • Gong, Y.1    Kakihara, Y.2    Krogan, N.3    Greenblatt, J.4    Emili, A.5    Zhang, Z.6    Houry, W.A.7
  • 37
    • 0033367325 scopus 로고    scopus 로고
    • Ribosome synthesis in Saccharomyces cerevisiae
    • Venema J., Tollervey D. Ribosome synthesis in Saccharomyces cerevisiae. Annu. Rev. Genet. 1999, 33:261-311.
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 261-311
    • Venema, J.1    Tollervey, D.2
  • 38
    • 0036591884 scopus 로고    scopus 로고
    • Biogenesis of small nucleolar ribonucleoproteins
    • Filipowicz W., Pogacic V. Biogenesis of small nucleolar ribonucleoproteins. Curr. Opin. Cell Biol. 2002, 14:319-327.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 319-327
    • Filipowicz, W.1    Pogacic, V.2
  • 39
    • 0030963268 scopus 로고    scopus 로고
    • Function and synthesis of small nucleolar RNAs
    • Tollervey D., Kiss T. Function and synthesis of small nucleolar RNAs. Curr. Opin. Cell Biol. 1997, 9:337-342.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 337-342
    • Tollervey, D.1    Kiss, T.2
  • 40
    • 0033153297 scopus 로고    scopus 로고
    • Guided tours: from precursor snoRNA to functional snoRNP
    • Weinstein L.B., Steitz J.A. Guided tours: from precursor snoRNA to functional snoRNP. Curr. Opin. Cell Biol. 1999, 11:378-384.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 378-384
    • Weinstein, L.B.1    Steitz, J.A.2
  • 41
    • 0034524515 scopus 로고    scopus 로고
    • Cajal bodies: the first 100 years
    • Gall J.G. Cajal bodies: the first 100 years. Annu. Rev. Cell Dev. Biol. 2000, 16:273-300.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 273-300
    • Gall, J.G.1
  • 42
    • 0035477838 scopus 로고    scopus 로고
    • Box C/D small nucleolar RNA trafficking involves small nucleolar RNP proteins, nucleolar factors and a novel nuclear domain
    • Verheggen C., Mouaikel J., Thiry M., Blanchard J.M., Tollervey D., Bordonne R., Lafontaine D.L., Bertrand E. Box C/D small nucleolar RNA trafficking involves small nucleolar RNP proteins, nucleolar factors and a novel nuclear domain. EMBO J. 2001, 20:5480-5490.
    • (2001) EMBO J. , vol.20 , pp. 5480-5490
    • Verheggen, C.1    Mouaikel, J.2    Thiry, M.3    Blanchard, J.M.4    Tollervey, D.5    Bordonne, R.6    Lafontaine, D.L.7    Bertrand, E.8
  • 44
    • 3242707680 scopus 로고    scopus 로고
    • Coupling between snoRNP assembly and 3' processing controls box C/D snoRNA biosynthesis in yeast
    • Morlando M., Ballarino M., Greco P., Caffarelli E., Dichtl B., Bozzoni I. Coupling between snoRNP assembly and 3' processing controls box C/D snoRNA biosynthesis in yeast. EMBO J. 2004, 23:2392-2401.
    • (2004) EMBO J. , vol.23 , pp. 2392-2401
    • Morlando, M.1    Ballarino, M.2    Greco, P.3    Caffarelli, E.4    Dichtl, B.5    Bozzoni, I.6
  • 45
    • 20744440616 scopus 로고    scopus 로고
    • The cotranscriptional assembly of snoRNPs controls the biosynthesis of H/ACA snoRNAs in Saccharomyces cerevisiae
    • Ballarino M., Morlando M., Pagano F., Fatica A., Bozzoni I. The cotranscriptional assembly of snoRNPs controls the biosynthesis of H/ACA snoRNAs in Saccharomyces cerevisiae. Mol. Cell. Biol. 2005, 25:5396-5403.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5396-5403
    • Ballarino, M.1    Morlando, M.2    Pagano, F.3    Fatica, A.4    Bozzoni, I.5
  • 46
    • 0036889385 scopus 로고    scopus 로고
    • Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP
    • Watkins N.J., Dickmanns A., Luhrmann R. Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP. Mol. Cell. Biol. 2002, 22:8342-8352.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8342-8352
    • Watkins, N.J.1    Dickmanns, A.2    Luhrmann, R.3
  • 47
    • 0034001337 scopus 로고    scopus 로고
    • Conserved composition of mammalian box H/ACA and box C/D small nucleolar ribonucleoprotein particles and their interaction with the common factor Nopp 140
    • Yang Y., Isaac C., Wang C., Dragon F., Pogacic V., Meier U.T. Conserved composition of mammalian box H/ACA and box C/D small nucleolar ribonucleoprotein particles and their interaction with the common factor Nopp 140. Mol. Biol. Cell 2000, 11:567-577.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 567-577
    • Yang, Y.1    Isaac, C.2    Wang, C.3    Dragon, F.4    Pogacic, V.5    Meier, U.T.6
  • 48
    • 0035943003 scopus 로고    scopus 로고
    • The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1
    • Pellizzoni L., Baccon J., Charroux B., Dreyfuss G. The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1. Curr. Biol. 2001, 11:1079-1088.
    • (2001) Curr. Biol. , vol.11 , pp. 1079-1088
    • Pellizzoni, L.1    Baccon, J.2    Charroux, B.3    Dreyfuss, G.4
  • 50
    • 34249317189 scopus 로고    scopus 로고
    • Novel subunits of the mammalian Hsp90 signal transduction chaperone
    • Te J., Jia L., Rogers J., Miller A., Hartson S.D. Novel subunits of the mammalian Hsp90 signal transduction chaperone. J. Proteome Res. 2007, 6:1963-1973.
    • (2007) J. Proteome Res. , vol.6 , pp. 1963-1973
    • Te, J.1    Jia, L.2    Rogers, J.3    Miller, A.4    Hartson, S.D.5
  • 52
    • 12544251380 scopus 로고    scopus 로고
    • Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing
    • Gonzales F.A., Zanchin N.I., Luz J.S., Oliveira C.C. Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing. J. Mol. Biol. 2005, 346:437-455.
    • (2005) J. Mol. Biol. , vol.346 , pp. 437-455
    • Gonzales, F.A.1    Zanchin, N.I.2    Luz, J.S.3    Oliveira, C.C.4
  • 53
    • 24644440130 scopus 로고    scopus 로고
    • Nop53p, an essential nucleolar protein that interacts with Nop17p and Nip7p, is required for pre-rRNA processing in Saccharomyces cerevisiae
    • Granato D.C., Gonzales F.A., Luz J.S., Cassiola F., Machado-Santelli G.M., Oliveira C.C. Nop53p, an essential nucleolar protein that interacts with Nop17p and Nip7p, is required for pre-rRNA processing in Saccharomyces cerevisiae. FEBS J. 2005, 272:4450-4463.
    • (2005) FEBS J. , vol.272 , pp. 4450-4463
    • Granato, D.C.1    Gonzales, F.A.2    Luz, J.S.3    Cassiola, F.4    Machado-Santelli, G.M.5    Oliveira, C.C.6
  • 54
    • 67849097183 scopus 로고    scopus 로고
    • High-resolution mapping of the protein interaction network for the human transcription machinery and affinity purification of RNA polymerase II-associated complexes
    • Cloutier P., Al-Khoury R., Lavallee-Adam M., Faubert D., Jiang H., Poitras C., Bouchard A., Forget D., Blanchette M., Coulombe B. High-resolution mapping of the protein interaction network for the human transcription machinery and affinity purification of RNA polymerase II-associated complexes. Methods 2009, 48:381-386.
    • (2009) Methods , vol.48 , pp. 381-386
    • Cloutier, P.1    Al-Khoury, R.2    Lavallee-Adam, M.3    Faubert, D.4    Jiang, H.5    Poitras, C.6    Bouchard, A.7    Forget, D.8    Blanchette, M.9    Coulombe, B.10
  • 57
    • 0020196749 scopus 로고
    • Radiation-sensitive mutants of Caenorhabditis elegans
    • Hartman P.S., Herman R.K. Radiation-sensitive mutants of Caenorhabditis elegans. Genetics 1982, 102:159-178.
    • (1982) Genetics , vol.102 , pp. 159-178
    • Hartman, P.S.1    Herman, R.K.2
  • 58
    • 0032829895 scopus 로고    scopus 로고
    • Tel2p, a regulator of yeast telomeric length in vivo, binds to single-stranded telomeric DNA in vitro
    • Kota R.S., Runge K.W. Tel2p, a regulator of yeast telomeric length in vivo, binds to single-stranded telomeric DNA in vitro. Chromosoma 1999, 108:278-290.
    • (1999) Chromosoma , vol.108 , pp. 278-290
    • Kota, R.S.1    Runge, K.W.2
  • 59
    • 0035846599 scopus 로고    scopus 로고
    • C. elegans RAD-5/CLK-2 defines a new DNA damage checkpoint protein
    • Ahmed S., Alpi A., Hengartner M.O., Gartner A. C. elegans RAD-5/CLK-2 defines a new DNA damage checkpoint protein. Curr. Biol. 2001, 11:1934-1944.
    • (2001) Curr. Biol. , vol.11 , pp. 1934-1944
    • Ahmed, S.1    Alpi, A.2    Hengartner, M.O.3    Gartner, A.4
  • 61
    • 34247158238 scopus 로고    scopus 로고
    • Tel2 is required for activation of the Mrc1-mediated replication checkpoint
    • Shikata M., Ishikawa F., Kanoh J. Tel2 is required for activation of the Mrc1-mediated replication checkpoint. J. Biol. Chem. 2007, 282:5346-5355.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5346-5355
    • Shikata, M.1    Ishikawa, F.2    Kanoh, J.3
  • 62
    • 37349014081 scopus 로고    scopus 로고
    • Tel2 regulates the stability of PI3K-related protein kinases
    • Takai H., Wang R.C., Takai K.K., Yang H., de Lange T. Tel2 regulates the stability of PI3K-related protein kinases. Cell 2007, 131:1248-1259.
    • (2007) Cell , vol.131 , pp. 1248-1259
    • Takai, H.1    Wang, R.C.2    Takai, K.K.3    Yang, H.4    de Lange, T.5
  • 63
    • 70350324640 scopus 로고    scopus 로고
    • Emerging common themes in regulation of PIKKs and PI3Ks
    • Lempiainen H., Halazonetis T.D. Emerging common themes in regulation of PIKKs and PI3Ks. EMBO J. 2009, 28:3067-3073.
    • (2009) EMBO J. , vol.28 , pp. 3067-3073
    • Lempiainen, H.1    Halazonetis, T.D.2
  • 64
    • 0037365789 scopus 로고    scopus 로고
    • ATM and related protein kinases: safeguarding genome integrity
    • Shiloh Y. ATM and related protein kinases: safeguarding genome integrity. Nat. Rev. Cancer 2003, 3:155-168.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 155-168
    • Shiloh, Y.1
  • 65
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S., Loewith R., Hall M.N. TOR signaling in growth and metabolism. Cell 2006, 124:471-484.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 66
    • 29144507015 scopus 로고    scopus 로고
    • The role of SMG-1 in nonsense-mediated mRNA decay
    • Yamashita A., Kashima I., Ohno S. The role of SMG-1 in nonsense-mediated mRNA decay. Biochim. Biophys. Acta 2005, 1754:305-315.
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 305-315
    • Yamashita, A.1    Kashima, I.2    Ohno, S.3
  • 67
    • 0032493894 scopus 로고    scopus 로고
    • The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins
    • McMahon S.B., Van Buskirk H.A., Dugan K.A., Copeland T.D., Cole M.D. The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins. Cell 1998, 94:363-374.
    • (1998) Cell , vol.94 , pp. 363-374
    • McMahon, S.B.1    Van Buskirk, H.A.2    Dugan, K.A.3    Copeland, T.D.4    Cole, M.D.5
  • 69
    • 77956856907 scopus 로고    scopus 로고
    • Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes
    • Takai H., Xie Y., de Lange T., Pavletich N.P. Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes. Genes Dev. 2010, 24:2019-2030.
    • (2010) Genes Dev. , vol.24 , pp. 2019-2030
    • Takai, H.1    Xie, Y.2    de Lange, T.3    Pavletich, N.P.4
  • 70
    • 0037567268 scopus 로고    scopus 로고
    • Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
    • Zou L., Elledge S.J. Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes. Science 2003, 300:1542-1548.
    • (2003) Science , vol.300 , pp. 1542-1548
    • Zou, L.1    Elledge, S.J.2
  • 73
    • 0033766666 scopus 로고    scopus 로고
    • Cdc13 cooperates with the yeast Ku proteins and Stn1 to regulate telomerase recruitment
    • Grandin N., Damon C., Charbonneau M. Cdc13 cooperates with the yeast Ku proteins and Stn1 to regulate telomerase recruitment. Mol. Cell. Biol. 2000, 20:8397-8408.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8397-8408
    • Grandin, N.1    Damon, C.2    Charbonneau, M.3
  • 74
    • 0035115859 scopus 로고    scopus 로고
    • Cdc13 both positively and negatively regulates telomere replication
    • Chandra A., Hughes T.R., Nugent C.I., Lundblad V. Cdc13 both positively and negatively regulates telomere replication. Genes Dev. 2001, 15:404-414.
    • (2001) Genes Dev. , vol.15 , pp. 404-414
    • Chandra, A.1    Hughes, T.R.2    Nugent, C.I.3    Lundblad, V.4
  • 75
    • 0035830494 scopus 로고    scopus 로고
    • Cdc13 delivers separate complexes to the telomere for end protection and replication
    • Pennock E., Buckley K., Lundblad V. Cdc13 delivers separate complexes to the telomere for end protection and replication. Cell 2001, 104:387-396.
    • (2001) Cell , vol.104 , pp. 387-396
    • Pennock, E.1    Buckley, K.2    Lundblad, V.3
  • 77
    • 77249158324 scopus 로고    scopus 로고
    • Curcumin inhibits nuclear localization of telomerase by dissociating the Hsp90 co-chaperone p23 from hTERT
    • Lee J.H., Chung I.K. Curcumin inhibits nuclear localization of telomerase by dissociating the Hsp90 co-chaperone p23 from hTERT. Cancer Lett. 2010, 290:76-86.
    • (2010) Cancer Lett. , vol.290 , pp. 76-86
    • Lee, J.H.1    Chung, I.K.2
  • 78
    • 78650632231 scopus 로고    scopus 로고
    • CHIP promotes human telomerase reverse transcriptase degradation and negatively regulates telomerase activity
    • Lee J.H., Khadka P., Baek S.H., Chung I.K. CHIP promotes human telomerase reverse transcriptase degradation and negatively regulates telomerase activity. J. Biol. Chem. 2010, 285:42033-42045.
    • (2010) J. Biol. Chem. , vol.285 , pp. 42033-42045
    • Lee, J.H.1    Khadka, P.2    Baek, S.H.3    Chung, I.K.4
  • 79
    • 79955119630 scopus 로고    scopus 로고
    • Inhibition of HSP90-dependent telomerase activity in amyloid beta-induced apoptosis of cerebral endothelial cells
    • Chiu W.T., Shen S.C., Yang L.Y., Chow J.M., Wu C.Y., Chen Y.C. Inhibition of HSP90-dependent telomerase activity in amyloid beta-induced apoptosis of cerebral endothelial cells. J. Cell. Physiol. 2011, 226:2041-2051.
    • (2011) J. Cell. Physiol. , vol.226 , pp. 2041-2051
    • Chiu, W.T.1    Shen, S.C.2    Yang, L.Y.3    Chow, J.M.4    Wu, C.Y.5    Chen, Y.C.6
  • 80
    • 37549046440 scopus 로고    scopus 로고
    • The hsp90 molecular chaperone modulates multiple telomerase activities
    • Toogun O.A., Dezwaan D.C., Freeman B.C. The hsp90 molecular chaperone modulates multiple telomerase activities. Mol. Cell. Biol. 2008, 28:457-467.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 457-467
    • Toogun, O.A.1    Dezwaan, D.C.2    Freeman, B.C.3
  • 81
    • 0035090016 scopus 로고    scopus 로고
    • Hsp90 levels affect telomere length in yeast
    • Grandin N., Charbonneau M. Hsp90 levels affect telomere length in yeast. Mol. Genet. Genomics 2001, 265:126-134.
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 126-134
    • Grandin, N.1    Charbonneau, M.2
  • 83
    • 0035844136 scopus 로고    scopus 로고
    • Stable association of hsp90 and p23, but not hsp70, with active human telomerase
    • Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E. Stable association of hsp90 and p23, but not hsp70, with active human telomerase. J. Biol. Chem. 2001, 276:15571-15574.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15571-15574
    • Forsythe, H.L.1    Jarvis, J.L.2    Turner, J.W.3    Elmore, L.W.4    Holt, S.E.5
  • 84
    • 33746030307 scopus 로고    scopus 로고
    • The biochemical role of the heat shock protein 90 chaperone complex in establishing human telomerase activity
    • Keppler B.R., Grady A.T., Jarstfer M.B. The biochemical role of the heat shock protein 90 chaperone complex in establishing human telomerase activity. J. Biol. Chem. 2006, 281:19840-19848.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19840-19848
    • Keppler, B.R.1    Grady, A.T.2    Jarstfer, M.B.3
  • 85
    • 77249158324 scopus 로고    scopus 로고
    • Curcumin inhibits nuclear localization of telomerase by dissociating the Hsp90 co-chaperone p23 from hTERT
    • Lee J.H., Chung I.K. Curcumin inhibits nuclear localization of telomerase by dissociating the Hsp90 co-chaperone p23 from hTERT. Cancer Lett. 2009, 290:76-86.
    • (2009) Cancer Lett. , vol.290 , pp. 76-86
    • Lee, J.H.1    Chung, I.K.2
  • 86
    • 0031451181 scopus 로고    scopus 로고
    • Probing the architecture of a simple kinetochore using DNA-protein crosslinking
    • Espelin C.W., Kaplan K.B., Sorger P.K. Probing the architecture of a simple kinetochore using DNA-protein crosslinking. J. Cell Biol. 1997, 139:1383-1396.
    • (1997) J. Cell Biol. , vol.139 , pp. 1383-1396
    • Espelin, C.W.1    Kaplan, K.B.2    Sorger, P.K.3
  • 87
    • 0030662073 scopus 로고    scopus 로고
    • Regulating the yeast kinetochore by ubiquitin-dependent degradation and Skp1p-mediated phosphorylation
    • Kaplan K.B., Hyman A.A., Sorger P.K. Regulating the yeast kinetochore by ubiquitin-dependent degradation and Skp1p-mediated phosphorylation. Cell 1997, 91:491-500.
    • (1997) Cell , vol.91 , pp. 491-500
    • Kaplan, K.B.1    Hyman, A.A.2    Sorger, P.K.3
  • 88
    • 0026013226 scopus 로고
    • A 240 kd multisubunit protein complex, CBF3, is a major component of the budding yeast centromere
    • Lechner J., Carbon J. A 240 kd multisubunit protein complex, CBF3, is a major component of the budding yeast centromere. Cell 1991, 64:717-725.
    • (1991) Cell , vol.64 , pp. 717-725
    • Lechner, J.1    Carbon, J.2
  • 89
    • 32044466689 scopus 로고    scopus 로고
    • The role of centromere-binding factor 3 (CBF3) in spindle stability, cytokinesis, and kinetochore attachment
    • Bouck D., Bloom K. The role of centromere-binding factor 3 (CBF3) in spindle stability, cytokinesis, and kinetochore attachment. Biochem. Cell Biol. 2005, 83:696-702.
    • (2005) Biochem. Cell Biol. , vol.83 , pp. 696-702
    • Bouck, D.1    Bloom, K.2
  • 90
    • 4744356146 scopus 로고    scopus 로고
    • The interaction between Sgt1p and Skp1p is regulated by HSP90 chaperones and is required for proper CBF3 assembly
    • Lingelbach L.B., Kaplan K.B. The interaction between Sgt1p and Skp1p is regulated by HSP90 chaperones and is required for proper CBF3 assembly. Mol. Cell. Biol. 2004, 24:8938-8950.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8938-8950
    • Lingelbach, L.B.1    Kaplan, K.B.2
  • 91
    • 3042842156 scopus 로고    scopus 로고
    • Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes required for proper kinetochore function
    • Rodrigo-Brenni M.C., Thomas S., Bouck D.C., Kaplan K.B. Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes required for proper kinetochore function. Mol. Biol. Cell 2004, 15:3366-3378.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3366-3378
    • Rodrigo-Brenni, M.C.1    Thomas, S.2    Bouck, D.C.3    Kaplan, K.B.4
  • 92
    • 77951198477 scopus 로고    scopus 로고
    • Hsp90-Sgt1 and Skp1 target human Mis12 complexes to ensure efficient formation of kinetochore-microtubule binding sites
    • Davies A.E., Kaplan K.B. Hsp90-Sgt1 and Skp1 target human Mis12 complexes to ensure efficient formation of kinetochore-microtubule binding sites. J. Cell Biol. 2010, 189:261-274.
    • (2010) J. Cell Biol. , vol.189 , pp. 261-274
    • Davies, A.E.1    Kaplan, K.B.2
  • 93
    • 4644242349 scopus 로고    scopus 로고
    • RNA silencing in plants
    • Baulcombe D. RNA silencing in plants. Nature 2004, 431:356-363.
    • (2004) Nature , vol.431 , pp. 356-363
    • Baulcombe, D.1
  • 94
    • 60149098474 scopus 로고    scopus 로고
    • Small RNAs as guardians of the genome
    • Malone C.D., Hannon G.J. Small RNAs as guardians of the genome. Cell 2009, 136:656-668.
    • (2009) Cell , vol.136 , pp. 656-668
    • Malone, C.D.1    Hannon, G.J.2
  • 95
    • 14644393684 scopus 로고    scopus 로고
    • Perspective: machines for RNAi
    • Tomari Y., Zamore P.D. Perspective: machines for RNAi. Genes Dev. 2005, 19:517-529.
    • (2005) Genes Dev. , vol.19 , pp. 517-529
    • Tomari, Y.1    Zamore, P.D.2
  • 96
    • 0141868916 scopus 로고    scopus 로고
    • R2D2, a bridge between the initiation and effector steps of the Drosophila RNAi pathway
    • Liu Q., Rand T.A., Kalidas S., Du F., Kim H.E., Smith D.P., Wang X. R2D2, a bridge between the initiation and effector steps of the Drosophila RNAi pathway. Science 2003, 301:1921-1925.
    • (2003) Science , vol.301 , pp. 1921-1925
    • Liu, Q.1    Rand, T.A.2    Kalidas, S.3    Du, F.4    Kim, H.E.5    Smith, D.P.6    Wang, X.7
  • 98
    • 27744477630 scopus 로고    scopus 로고
    • Molecular requirements for RNA-induced silencing complex assembly in the Drosophila RNA interference pathway
    • Pham J.W., Sontheimer E.J. Molecular requirements for RNA-induced silencing complex assembly in the Drosophila RNA interference pathway. J. Biol. Chem. 2005, 280:39278-39283.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39278-39283
    • Pham, J.W.1    Sontheimer, E.J.2
  • 99
    • 33746581711 scopus 로고    scopus 로고
    • Dicer-2 and R2D2 coordinately bind siRNA to promote assembly of the siRISC complexes
    • Liu X., Jiang F., Kalidas S., Smith D., Liu Q. Dicer-2 and R2D2 coordinately bind siRNA to promote assembly of the siRISC complexes. RNA 2006, 12:1514-1520.
    • (2006) RNA , vol.12 , pp. 1514-1520
    • Liu, X.1    Jiang, F.2    Kalidas, S.3    Smith, D.4    Liu, Q.5
  • 100
    • 27744590896 scopus 로고    scopus 로고
    • Passenger-strand cleavage facilitates assembly of siRNA into Ago2-containing RNAi enzyme complexes
    • Matranga C., Tomari Y., Shin C., Bartel D.P., Zamore P.D. Passenger-strand cleavage facilitates assembly of siRNA into Ago2-containing RNAi enzyme complexes. Cell 2005, 123:607-620.
    • (2005) Cell , vol.123 , pp. 607-620
    • Matranga, C.1    Tomari, Y.2    Shin, C.3    Bartel, D.P.4    Zamore, P.D.5
  • 101
    • 60149088848 scopus 로고    scopus 로고
    • Origins and mechanisms of miRNAs and siRNAs
    • Carthew R.W., Sontheimer E.J. Origins and mechanisms of miRNAs and siRNAs. Cell 2009, 136:642-655.
    • (2009) Cell , vol.136 , pp. 642-655
    • Carthew, R.W.1    Sontheimer, E.J.2
  • 102
    • 1642487115 scopus 로고    scopus 로고
    • Characterization of the interactions between mammalian PAZ PIWI domain proteins and Dicer
    • Tahbaz N., Kolb F.A., Zhang H., Jaronczyk K., Filipowicz W., Hobman T.C. Characterization of the interactions between mammalian PAZ PIWI domain proteins and Dicer. EMBO Rep. 2004, 5:189-194.
    • (2004) EMBO Rep. , vol.5 , pp. 189-194
    • Tahbaz, N.1    Kolb, F.A.2    Zhang, H.3    Jaronczyk, K.4    Filipowicz, W.5    Hobman, T.C.6
  • 103
    • 77951712353 scopus 로고    scopus 로고
    • HSP90 protein stabilizes unloaded argonaute complexes and microscopic P-bodies in human cells
    • Johnston M., Geoffroy M.C., Sobala A., Hay R., Hutvagner G. HSP90 protein stabilizes unloaded argonaute complexes and microscopic P-bodies in human cells. Mol. Biol. Cell 2010, 21:1462-1469.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1462-1469
    • Johnston, M.1    Geoffroy, M.C.2    Sobala, A.3    Hay, R.4    Hutvagner, G.5
  • 106
    • 0034791090 scopus 로고    scopus 로고
    • Ubiquitin enters the new millennium
    • Pickart C.M. Ubiquitin enters the new millennium. Mol. Cell 2001, 8:499-504.
    • (2001) Mol. Cell , vol.8 , pp. 499-504
    • Pickart, C.M.1
  • 107
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: paradigm of a self-compartmentalizing protease
    • Baumeister W., Walz J., Zuhl F., Seemuller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 1998, 92:367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 108
    • 0042313977 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome
    • Imai J., Maruya M., Yashiroda H., Yahara I., Tanaka K. The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J. 2003, 22:3557-3567.
    • (2003) EMBO J. , vol.22 , pp. 3557-3567
    • Imai, J.1    Maruya, M.2    Yashiroda, H.3    Yahara, I.4    Tanaka, K.5
  • 109
    • 57649118512 scopus 로고    scopus 로고
    • Hsp90-mediated assembly of the 26 S proteasome is involved in major histocompatibility complex class I antigen processing
    • Yamano T., Mizukami S., Murata S., Chiba T., Tanaka K., Udono H. Hsp90-mediated assembly of the 26 S proteasome is involved in major histocompatibility complex class I antigen processing. J. Biol. Chem. 2008, 283:28060-28065.
    • (2008) J. Biol. Chem. , vol.283 , pp. 28060-28065
    • Yamano, T.1    Mizukami, S.2    Murata, S.3    Chiba, T.4    Tanaka, K.5    Udono, H.6


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