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Volumn 159, Issue 6, 2014, Pages 1389-1403

Proteostatic control of telomerase function through TRiC-mediated folding of TCAB1

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN CONTAINING TCP1; PROTEIN; PROTEIN TCAB1; RNA; SMALL CAJAL BODY RNA; SMALL INTERFERING RNA; TELOMERASE; UNCLASSIFIED DRUG; TELOMERASE CAJAL BODY PROTEIN 1, HUMAN;

EID: 84923591348     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2014.10.059     Document Type: Article
Times cited : (114)

References (52)
  • 2
    • 30344462410 scopus 로고    scopus 로고
    • Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    • V. Albanèse, A.Y.-W. Yam, J. Baughman, C. Parnot, and J. Frydman Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells Cell 124 2006 75 88
    • (2006) Cell , vol.124 , pp. 75-88
    • Albanèse, V.1    Yam, A.Y.-W.2    Baughman, J.3    Parnot, C.4    Frydman, J.5
  • 4
    • 74049111326 scopus 로고    scopus 로고
    • Telomeres and telomerase in cancer
    • S.E. Artandi, and R.A. DePinho Telomeres and telomerase in cancer Carcinogenesis 31 2010 9 18
    • (2010) Carcinogenesis , vol.31 , pp. 9-18
    • Artandi, S.E.1    Depinho, R.A.2
  • 5
    • 84883816534 scopus 로고    scopus 로고
    • Understanding telomere diseases through analysis of patient-derived iPS cells
    • L.F. Batista, and S.E. Artandi Understanding telomere diseases through analysis of patient-derived iPS cells Curr. Opin. Genet. Dev. 23 2013 526 533
    • (2013) Curr. Opin. Genet. Dev. , vol.23 , pp. 526-533
    • Batista, L.F.1    Artandi, S.E.2
  • 7
    • 34147095342 scopus 로고    scopus 로고
    • Protein composition of catalytically active human telomerase from immortal cells
    • S.B. Cohen, M.E. Graham, G.O. Lovrecz, N. Bache, P.J. Robinson, and R.R. Reddel Protein composition of catalytically active human telomerase from immortal cells Science 315 2007 1850 1853
    • (2007) Science , vol.315 , pp. 1850-1853
    • Cohen, S.B.1    Graham, M.E.2    Lovrecz, G.O.3    Bache, N.4    Robinson, P.J.5    Reddel, R.R.6
  • 8
    • 32544443342 scopus 로고    scopus 로고
    • Telomere length homeostasis requires that telomerase levels are limiting
    • G. Cristofari, and J. Lingner Telomere length homeostasis requires that telomerase levels are limiting EMBO J. 25 2006 565 574
    • (2006) EMBO J. , vol.25 , pp. 565-574
    • Cristofari, G.1    Lingner, J.2
  • 9
    • 34748876539 scopus 로고    scopus 로고
    • Human telomerase RNA accumulation in Cajal bodies facilitates telomerase recruitment to telomeres and telomere elongation
    • G. Cristofari, E. Adolf, P. Reichenbach, K. Sikora, R.M. Terns, M.P. Terns, and J. Lingner Human telomerase RNA accumulation in Cajal bodies facilitates telomerase recruitment to telomeres and telomere elongation Mol. Cell 27 2007 882 889
    • (2007) Mol. Cell , vol.27 , pp. 882-889
    • Cristofari, G.1    Adolf, E.2    Reichenbach, P.3    Sikora, K.4    Terns, R.M.5    Terns, M.P.6    Lingner, J.7
  • 10
    • 0037013831 scopus 로고    scopus 로고
    • Cajal body-specific small nuclear RNAs: A novel class of 2′-O-methylation and pseudouridylation guide RNAs
    • X. Darzacq, B.E. Jády, C. Verheggen, A.M. Kiss, E. Bertrand, and T. Kiss Cajal body-specific small nuclear RNAs: a novel class of 2′-O-methylation and pseudouridylation guide RNAs EMBO J. 21 2002 2746 2756
    • (2002) EMBO J. , vol.21 , pp. 2746-2756
    • Darzacq, X.1    Jády, B.E.2    Verheggen, C.3    Kiss, A.M.4    Bertrand, E.5    Kiss, T.6
  • 12
    • 84866611481 scopus 로고    scopus 로고
    • Biogenesis of telomerase ribonucleoproteins
    • E.D. Egan, and K. Collins Biogenesis of telomerase ribonucleoproteins RNA 18 2012 1747 1759
    • (2012) RNA , vol.18 , pp. 1747-1759
    • Egan, E.D.1    Collins, K.2
  • 13
    • 0345708112 scopus 로고    scopus 로고
    • Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding
    • D.E. Feldman, C. Spiess, D.E. Howard, and J. Frydman Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding Mol. Cell 12 2003 1213 1224
    • (2003) Mol. Cell , vol.12 , pp. 1213-1224
    • Feldman, D.E.1    Spiess, C.2    Howard, D.E.3    Frydman, J.4
  • 14
    • 0027077442 scopus 로고
    • Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
    • J. Frydman, E. Nimmesgern, H. Erdjument-Bromage, J.S. Wall, P. Tempst, and F.U. Hartl Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits EMBO J. 11 1992 4767 4778
    • (1992) EMBO J. , vol.11 , pp. 4767-4778
    • Frydman, J.1    Nimmesgern, E.2    Erdjument-Bromage, H.3    Wall, J.S.4    Tempst, P.5    Hartl, F.U.6
  • 15
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • J. Frydman, E. Nimmesgern, K. Ohtsuka, and F.U. Hartl Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones Nature 370 1994 111 117
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 16
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes beta-actin folding
    • Y. Gao, J.O. Thomas, R.L. Chow, G.H. Lee, and N.J. Cowan A cytoplasmic chaperonin that catalyzes beta-actin folding Cell 69 1992 1043 1050
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 18
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • F.U. Hartl, A. Bracher, and M. Hayer-Hartl Molecular chaperones in protein folding and proteostasis Nature 475 2011 324 332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 23
    • 17944388104 scopus 로고    scopus 로고
    • Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal
    • B.E. Jády, E. Bertrand, and T. Kiss Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal J. Cell Biol. 164 2004 647 652
    • (2004) J. Cell Biol. , vol.164 , pp. 647-652
    • Jády, B.E.1    Bertrand, E.2    Kiss, T.3
  • 27
    • 0031018154 scopus 로고    scopus 로고
    • Tissue-specific subunit of the mouse cytosolic chaperonin-containing TCP-1
    • H. Kubota, G.M. Hynes, S.M. Kerr, and K.R. Willison Tissue-specific subunit of the mouse cytosolic chaperonin-containing TCP-1 FEBS Lett. 402 1997 53 56
    • (1997) FEBS Lett. , vol.402 , pp. 53-56
    • Kubota, H.1    Hynes, G.M.2    Kerr, S.M.3    Willison, K.R.4
  • 28
    • 84867840534 scopus 로고    scopus 로고
    • Comprehensive review on the HSC70 functions, interactions with related molecules and involvement in clinical diseases and therapeutic potential
    • T. Liu, C.K. Daniels, and S. Cao Comprehensive review on the HSC70 functions, interactions with related molecules and involvement in clinical diseases and therapeutic potential Pharmacol. Ther. 136 2012 354 374
    • (2012) Pharmacol. Ther. , vol.136 , pp. 354-374
    • Liu, T.1    Daniels, C.K.2    Cao, S.3
  • 29
    • 0033518188 scopus 로고    scopus 로고
    • A telomerase component is defective in the human disease dyskeratosis congenita
    • J.R. Mitchell, E. Wood, and K. Collins A telomerase component is defective in the human disease dyskeratosis congenita Nature 402 1999 551 555
    • (1999) Nature , vol.402 , pp. 551-555
    • Mitchell, J.R.1    Wood, E.2    Collins, K.3
  • 30
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • R.I. Morimoto Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging Genes Dev. 22 2008 1427 1438
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 31
    • 84870980867 scopus 로고    scopus 로고
    • The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity
    • J. Nandakumar, C.F. Bell, I. Weidenfeld, A.J. Zaug, L.A. Leinwand, and T.R. Cech The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity Nature 492 2012 285 289
    • (2012) Nature , vol.492 , pp. 285-289
    • Nandakumar, J.1    Bell, C.F.2    Weidenfeld, I.3    Zaug, A.J.4    Leinwand, L.A.5    Cech, T.R.6
  • 32
    • 46249125488 scopus 로고    scopus 로고
    • How shelterin protects mammalian telomeres
    • W. Palm, and T. de Lange How shelterin protects mammalian telomeres Annu. Rev. Genet. 42 2008 301 334
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 301-334
    • Palm, W.1    De Lange, T.2
  • 33
    • 84877102552 scopus 로고    scopus 로고
    • Replication of telomeres and the regulation of telomerase
    • V. Pfeiffer, and J. Lingner Replication of telomeres and the regulation of telomerase Cold Spring Harb. Perspect. Biol. 5 2013 a010405
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5 , pp. a010405
    • Pfeiffer, V.1    Lingner, J.2
  • 34
    • 30744445688 scopus 로고    scopus 로고
    • Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita
    • R. Rashid, B. Liang, D.L. Baker, O.A. Youssef, Y. He, K. Phipps, R.M. Terns, M.P. Terns, and H. Li Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita Mol. Cell 21 2006 249 260
    • (2006) Mol. Cell , vol.21 , pp. 249-260
    • Rashid, R.1    Liang, B.2    Baker, D.L.3    Youssef, O.A.4    He, Y.5    Phipps, K.6    Terns, R.M.7    Terns, M.P.8    Li, H.9
  • 35
    • 84867243004 scopus 로고    scopus 로고
    • Specificity requirements for human telomere protein interaction with telomerase holoenzyme
    • A.N. Sexton, D.T. Youmans, and K. Collins Specificity requirements for human telomere protein interaction with telomerase holoenzyme J. Biol. Chem. 287 2012 34455 34464
    • (2012) J. Biol. Chem. , vol.287 , pp. 34455-34464
    • Sexton, A.N.1    Youmans, D.T.2    Collins, K.3
  • 36
    • 84864020175 scopus 로고    scopus 로고
    • Telomerase recruitment requires both TCAB1 and Cajal bodies independently
    • J.L. Stern, K.G. Zyner, H.A. Pickett, S.B. Cohen, and T.M. Bryan Telomerase recruitment requires both TCAB1 and Cajal bodies independently Mol. Cell. Biol. 32 2012 2384 2395
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 2384-2395
    • Stern, J.L.1    Zyner, K.G.2    Pickett, H.A.3    Cohen, S.B.4    Bryan, T.M.5
  • 37
    • 33749177252 scopus 로고    scopus 로고
    • The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
    • S. Tam, R. Geller, C. Spiess, and J. Frydman The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions Nat. Cell Biol. 8 2006 1155 1162
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1155-1162
    • Tam, S.1    Geller, R.2    Spiess, C.3    Frydman, J.4
  • 39
    • 63649111958 scopus 로고    scopus 로고
    • A conserved WD40 protein binds the Cajal body localization signal of scaRNP particles
    • K.T. Tycowski, M.D. Shu, A. Kukoyi, and J.A. Steitz A conserved WD40 protein binds the Cajal body localization signal of scaRNP particles Mol. Cell 34 2009 47 57
    • (2009) Mol. Cell , vol.34 , pp. 47-57
    • Tycowski, K.T.1    Shu, M.D.2    Kukoyi, A.3    Steitz, J.A.4
  • 41
    • 40749135820 scopus 로고    scopus 로고
    • Identification of ATPases pontin and reptin as telomerase components essential for holoenzyme assembly
    • A.S. Venteicher, Z. Meng, P.J. Mason, T.D. Veenstra, and S.E. Artandi Identification of ATPases pontin and reptin as telomerase components essential for holoenzyme assembly Cell 132 2008 945 957
    • (2008) Cell , vol.132 , pp. 945-957
    • Venteicher, A.S.1    Meng, Z.2    Mason, P.J.3    Veenstra, T.D.4    Artandi, S.E.5
  • 43
    • 84897129156 scopus 로고    scopus 로고
    • Differential scales of protein quality control
    • S. Wolff, J.S. Weissman, and A. Dillin Differential scales of protein quality control Cell 157 2014 52 64
    • (2014) Cell , vol.157 , pp. 52-64
    • Wolff, S.1    Weissman, J.S.2    Dillin, A.3
  • 44
    • 33751072682 scopus 로고    scopus 로고
    • Telomerase RNA level limits telomere maintenance in X-linked dyskeratosis congenita
    • J.M.Y. Wong, and K. Collins Telomerase RNA level limits telomere maintenance in X-linked dyskeratosis congenita Genes Dev. 20 2006 2848 2858
    • (2006) Genes Dev. , vol.20 , pp. 2848-2858
    • Wong, J.M.Y.1    Collins, K.2
  • 45
    • 57149098022 scopus 로고    scopus 로고
    • Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
    • A.Y. Yam, Y. Xia, H.-T.J. Lin, A. Burlingame, M. Gerstein, and J. Frydman Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies Nat. Struct. Mol. Biol. 15 2008 1255 1262
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1255-1262
    • Yam, A.Y.1    Xia, Y.2    Lin, H.-T.J.3    Burlingame, A.4    Gerstein, M.5    Frydman, J.6
  • 46
  • 47
    • 0033003760 scopus 로고    scopus 로고
    • A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays
    • J.H. Zhang, T.D. Chung, and K.R. Oldenburg A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays J. Biomol. Screen. 4 1999 67 73
    • (1999) J. Biomol. Screen. , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 49
    • 84864607108 scopus 로고    scopus 로고
    • TPP1 OB-fold domain controls telomere maintenance by recruiting telomerase to chromosome ends
    • F.L. Zhong, L.F.Z. Batista, A. Freund, M.F. Pech, A.S. Venteicher, and S.E. Artandi TPP1 OB-fold domain controls telomere maintenance by recruiting telomerase to chromosome ends Cell 150 2012 481 494
    • (2012) Cell , vol.150 , pp. 481-494
    • Zhong, F.L.1    Batista, L.F.Z.2    Freund, A.3    Pech, M.F.4    Venteicher, A.S.5    Artandi, S.E.6
  • 52
    • 0034572910 scopus 로고    scopus 로고
    • Purification of the cytosolic chaperonin TRiC from bovine testis
    • R.G. Ferreyra, and J. Frydman Purification of the cytosolic chaperonin TRiC from bovine testis Methods Mol. Biol. 140 2000 153 160
    • (2000) Methods Mol. Biol. , vol.140 , pp. 153-160
    • Ferreyra, R.G.1    Frydman, J.2


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