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Volumn 388, Issue 5, 2009, Pages 928-940

Human PinX1 Mediates TRF1 Accumulation in Nucleolus and Enhances TRF1 Binding to Telomeres

Author keywords

ALT; human PinX1; nucleolus; telomere; TRF1

Indexed keywords

FIBRILLARIN; GREEN FLUORESCENT PROTEIN; HEMAGGLUTININ; MYC PROTEIN; TELOMERIC REPEAT BINDING FACTOR 1;

EID: 67349126168     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.02.051     Document Type: Article
Times cited : (20)

References (42)
  • 1
    • 0345687981 scopus 로고    scopus 로고
    • Composition and conservation of the telomeric complex
    • Kanoh J., and Ishikawa F. Composition and conservation of the telomeric complex. Cell Mol. Life Sci. 60 (2003) 2295-2302
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 2295-2302
    • Kanoh, J.1    Ishikawa, F.2
  • 2
    • 33745849998 scopus 로고    scopus 로고
    • The Structure and Function of Telomerase Reverse Transcriptase
    • Autexier C., and Lue N.F. The Structure and Function of Telomerase Reverse Transcriptase. Annu. Rev. Biochem. 75 (2006) 493-517
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 493-517
    • Autexier, C.1    Lue, N.F.2
  • 3
    • 24944460598 scopus 로고    scopus 로고
    • Shelterin: the protein complex that shapes and safeguards human telomeres
    • de Lange T. Shelterin: the protein complex that shapes and safeguards human telomeres. Genes Dev. 19 (2005) 2100-2110
    • (2005) Genes Dev. , vol.19 , pp. 2100-2110
    • de Lange, T.1
  • 4
    • 0031027618 scopus 로고    scopus 로고
    • Control of telomere length by the human telomeric protein TRF1
    • van Steensel B., and de Lange T. Control of telomere length by the human telomeric protein TRF1. Nature 385 (1997) 740-743
    • (1997) Nature , vol.385 , pp. 740-743
    • van Steensel, B.1    de Lange, T.2
  • 6
    • 0036241994 scopus 로고    scopus 로고
    • Targeting assay to study the cis functions of human telomeric proteins: evidence for inhibition of telomerase by TRF1 and for activation of telomere degradation by TRF2
    • Ancelin K., Brunori M., Bauwens S., Koering C.E., Brun C., Ricoul M., et al. Targeting assay to study the cis functions of human telomeric proteins: evidence for inhibition of telomerase by TRF1 and for activation of telomere degradation by TRF2. Mol. Cell Biol. 22 (2002) 3474-3487
    • (2002) Mol. Cell Biol. , vol.22 , pp. 3474-3487
    • Ancelin, K.1    Brunori, M.2    Bauwens, S.3    Koering, C.E.4    Brun, C.5    Ricoul, M.6
  • 7
    • 0032553473 scopus 로고    scopus 로고
    • Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
    • Smith S., Giriat I., Schmitt A., and de Lange T. Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. Science 282 (1998) 1484-1487
    • (1998) Science , vol.282 , pp. 1484-1487
    • Smith, S.1    Giriat, I.2    Schmitt, A.3    de Lange, T.4
  • 8
    • 0032727616 scopus 로고    scopus 로고
    • TIN2, a new regulator of telomere length in human cells
    • Kim S.H., Kaminker P., and Campisi J. TIN2, a new regulator of telomere length in human cells. Nature Genet. 23 (1999) 405-412
    • (1999) Nature Genet. , vol.23 , pp. 405-412
    • Kim, S.H.1    Kaminker, P.2    Campisi, J.3
  • 9
    • 0034669104 scopus 로고    scopus 로고
    • Ku acts in a unique way at the mammalian telomere to prevent end joining
    • Hsu H.L., Gilley D., Galande S.A., Hande M.P., Allen B., Kim S.H., et al. Ku acts in a unique way at the mammalian telomere to prevent end joining. Genes Dev. 14 (2000) 2807-2812
    • (2000) Genes Dev. , vol.14 , pp. 2807-2812
    • Hsu, H.L.1    Gilley, D.2    Galande, S.A.3    Hande, M.P.4    Allen, B.5    Kim, S.H.6
  • 10
    • 0035929591 scopus 로고    scopus 로고
    • TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression
    • Kaminker P.G., Kim S.H., Taylor R.D., Zebarjadian Y., Funk W.D., Morin G.B., et al. TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression. J. Biol. Chem. 276 (2001) 35891-35899
    • (2001) J. Biol. Chem. , vol.276 , pp. 35891-35899
    • Kaminker, P.G.1    Kim, S.H.2    Taylor, R.D.3    Zebarjadian, Y.4    Funk, W.D.5    Morin, G.B.6
  • 12
    • 2942637828 scopus 로고    scopus 로고
    • The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2
    • Opresko P.L., Otterlei M., Graakjaer J., Bruheim P., Dawut L., Kolvraa S., et al. The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2. Mol. Cell 14 (2004) 763-774
    • (2004) Mol. Cell , vol.14 , pp. 763-774
    • Opresko, P.L.1    Otterlei, M.2    Graakjaer, J.3    Bruheim, P.4    Dawut, L.5    Kolvraa, S.6
  • 13
    • 0036734655 scopus 로고    scopus 로고
    • The product of the survival of motor neuron (SMN) gene is a human telomerase-associated protein
    • Bachand F., Boisvert F.M., Cote J., Richard S., and Autexier C. The product of the survival of motor neuron (SMN) gene is a human telomerase-associated protein. Mol. Biol. Cell 13 (2002) 3192-3202
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3192-3202
    • Bachand, F.1    Boisvert, F.M.2    Cote, J.3    Richard, S.4    Autexier, C.5
  • 15
    • 17344363008 scopus 로고    scopus 로고
    • Telomerase activation by hTRT in human normal fibroblasts and hepatocellular carcinomas
    • Nakayama J., Tahara H., Tahara E., Saito M., Ito K., Nakamura H., et al. Telomerase activation by hTRT in human normal fibroblasts and hepatocellular carcinomas. Nature Genet. 18 (1998) 65-68
    • (1998) Nature Genet. , vol.18 , pp. 65-68
    • Nakayama, J.1    Tahara, H.2    Tahara, E.3    Saito, M.4    Ito, K.5    Nakamura, H.6
  • 16
    • 0030659644 scopus 로고    scopus 로고
    • Reconstitution of human telomerase with the template RNA component hTR and the catalytic protein subunit hTRT
    • Weinrich S.L., Pruzan R., Ma L., Ouellette M., Tesmer V.M., Holt S.E., et al. Reconstitution of human telomerase with the template RNA component hTR and the catalytic protein subunit hTRT. Nature Genet. 17 (1997) 498-502
    • (1997) Nature Genet. , vol.17 , pp. 498-502
    • Weinrich, S.L.1    Pruzan, R.2    Ma, L.3    Ouellette, M.4    Tesmer, V.M.5    Holt, S.E.6
  • 17
    • 0030745448 scopus 로고    scopus 로고
    • hEST2, the putative human telomerase catalytic subunit gene, is up-regulated in tumor cells and during immortalization
    • Meyerson M., Counter C.M., Eaton E.N., Ellisen L.W., Steiner P., Caddle S.D., et al. hEST2, the putative human telomerase catalytic subunit gene, is up-regulated in tumor cells and during immortalization. Cell 90 (1997) 785-795
    • (1997) Cell , vol.90 , pp. 785-795
    • Meyerson, M.1    Counter, C.M.2    Eaton, E.N.3    Ellisen, L.W.4    Steiner, P.5    Caddle, S.D.6
  • 18
    • 0032485416 scopus 로고    scopus 로고
    • Telomerase activity is restored in human cells by ectopic expression of hTERT (hEST2), the catalytic subunit of telomerase
    • Counter C.M., Meyerson M., Eaton E.N., Ellisen L.W., Caddle S.D., Haber D.A., and Weinberg R.A. Telomerase activity is restored in human cells by ectopic expression of hTERT (hEST2), the catalytic subunit of telomerase. Oncogene 16 (1998) 1217-1222
    • (1998) Oncogene , vol.16 , pp. 1217-1222
    • Counter, C.M.1    Meyerson, M.2    Eaton, E.N.3    Ellisen, L.W.4    Caddle, S.D.5    Haber, D.A.6    Weinberg, R.A.7
  • 20
    • 0036711651 scopus 로고    scopus 로고
    • Subnuclear shuttling of human telomerase induced by transformation and DNA damage
    • Wong J.M., Kusdra L., and Collins K. Subnuclear shuttling of human telomerase induced by transformation and DNA damage. Nature Cell Biol. 4 (2002) 731-736
    • (2002) Nature Cell Biol. , vol.4 , pp. 731-736
    • Wong, J.M.1    Kusdra, L.2    Collins, K.3
  • 21
    • 0036311278 scopus 로고    scopus 로고
    • Nucleolar localization of hTERT protein is associated with telomerase function
    • Yang Y., Chen Y., Zhang C., Huang H., and Weissman S.M. Nucleolar localization of hTERT protein is associated with telomerase function. Exp. Cell Res. 277 (2002) 201-209
    • (2002) Exp. Cell Res. , vol.277 , pp. 201-209
    • Yang, Y.1    Chen, Y.2    Zhang, C.3    Huang, H.4    Weissman, S.M.5
  • 23
    • 0035798379 scopus 로고    scopus 로고
    • The Pin2/TRF1-interacting protein PinX1 is a potent telomerase inhibitor
    • Zhou X.Z., and Lu K.P. The Pin2/TRF1-interacting protein PinX1 is a potent telomerase inhibitor. Cell 107 (2001) 347-359
    • (2001) Cell , vol.107 , pp. 347-359
    • Zhou, X.Z.1    Lu, K.P.2
  • 24
    • 0033803788 scopus 로고    scopus 로고
    • Identification of the gene for a novel liver-related putative tumor suppressor at a high-frequency loss of heterozygosity region of chromosome 8p23 in human hepatocellular carcinoma
    • Liao C., Zhao M., Song H., Uchida K., Yokoyama K.K., and Li T. Identification of the gene for a novel liver-related putative tumor suppressor at a high-frequency loss of heterozygosity region of chromosome 8p23 in human hepatocellular carcinoma. Hepatology 32 (2000) 721-727
    • (2000) Hepatology , vol.32 , pp. 721-727
    • Liao, C.1    Zhao, M.2    Song, H.3    Uchida, K.4    Yokoyama, K.K.5    Li, T.6
  • 25
    • 1542373680 scopus 로고    scopus 로고
    • Nucleolar protein PinX1p regulates telomerase by sequestering its protein catalytic subunit in an inactive complex lacking telomerase RNA
    • Lin J., and Blackburn E.H. Nucleolar protein PinX1p regulates telomerase by sequestering its protein catalytic subunit in an inactive complex lacking telomerase RNA. Genes Dev. 18 (2004) 387-396
    • (2004) Genes Dev. , vol.18 , pp. 387-396
    • Lin, J.1    Blackburn, E.H.2
  • 26
    • 34548014298 scopus 로고    scopus 로고
    • Rat homolog of PinX1 is a nucleolar protein involved in the regulation of telomere length
    • Oh B.K., Yoon S.M., Lee C.H., and Park Y.N. Rat homolog of PinX1 is a nucleolar protein involved in the regulation of telomere length. Gene 400 (2007) 35-43
    • (2007) Gene , vol.400 , pp. 35-43
    • Oh, B.K.1    Yoon, S.M.2    Lee, C.H.3    Park, Y.N.4
  • 27
    • 0037144620 scopus 로고    scopus 로고
    • The yeast homolog of human PinX1 is involved in rRNA and small nucleolar RNA maturation, not in telomere elongation inhibition
    • Guglielmi B., and Werner M. The yeast homolog of human PinX1 is involved in rRNA and small nucleolar RNA maturation, not in telomere elongation inhibition. J. Biol. Chem. 277 (2002) 35712-35719
    • (2002) J. Biol. Chem. , vol.277 , pp. 35712-35719
    • Guglielmi, B.1    Werner, M.2
  • 28
    • 1642338831 scopus 로고    scopus 로고
    • Human MCRS2, a cell-cycle-dependent protein, associates with LPTS/PinX1 and reduces the telomere length
    • Song H., Li Y., Chen G., Xing Z., Zhao J., Yokoyama K.K., et al. Human MCRS2, a cell-cycle-dependent protein, associates with LPTS/PinX1 and reduces the telomere length. Biochem. Biophys. Res. Commun. 316 (2004) 1116-1123
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 1116-1123
    • Song, H.1    Li, Y.2    Chen, G.3    Xing, Z.4    Zhao, J.5    Yokoyama, K.K.6
  • 29
    • 0023812595 scopus 로고
    • Sequence requirements for nucleolar localization of human T cell leukemia virus type I pX protein, which regulates viral RNA processing
    • Siomi H., Shida H., Nam S.H., Nosaka T., Maki M., and Hatanaka M. Sequence requirements for nucleolar localization of human T cell leukemia virus type I pX protein, which regulates viral RNA processing. Cell 55 (1988) 197-209
    • (1988) Cell , vol.55 , pp. 197-209
    • Siomi, H.1    Shida, H.2    Nam, S.H.3    Nosaka, T.4    Maki, M.5    Hatanaka, M.6
  • 30
    • 0028784029 scopus 로고
    • Nuclear and nucleolar targeting of human ribosomal protein S6
    • Schmidt C., Lipsius E., and Kruppa J. Nuclear and nucleolar targeting of human ribosomal protein S6. Mol. Biol. Cell 6 (1995) 1875-1885
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1875-1885
    • Schmidt, C.1    Lipsius, E.2    Kruppa, J.3
  • 31
    • 15844407348 scopus 로고    scopus 로고
    • Distinct domains in ribosomal protein L5 mediate 5 S rRNA binding and nucleolar localization
    • Michael W.M., and Dreyfuss G. Distinct domains in ribosomal protein L5 mediate 5 S rRNA binding and nucleolar localization. J. Biol. Chem. 271 (1996) 11571-11574
    • (1996) J. Biol. Chem. , vol.271 , pp. 11571-11574
    • Michael, W.M.1    Dreyfuss, G.2
  • 34
    • 31944436260 scopus 로고    scopus 로고
    • Cell cycle-dependent recruitment of telomerase RNA and Cajal bodies to human telomeres
    • Jady B.E., Richard P., Bertrand E., and Kiss T. Cell cycle-dependent recruitment of telomerase RNA and Cajal bodies to human telomeres. Mol. Biol. Cell 17 (2006) 944-954
    • (2006) Mol. Biol. Cell , vol.17 , pp. 944-954
    • Jady, B.E.1    Richard, P.2    Bertrand, E.3    Kiss, T.4
  • 36
    • 0037610123 scopus 로고    scopus 로고
    • TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
    • Chang W., Dynek J.N., and Smith S. TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres. Genes Dev. 17 (2003) 1328-1333
    • (2003) Genes Dev. , vol.17 , pp. 1328-1333
    • Chang, W.1    Dynek, J.N.2    Smith, S.3
  • 37
    • 34548492016 scopus 로고    scopus 로고
    • MRE11-RAD50-NBS1 and ATM function as co-mediators of TRF1 in telomere length control
    • Wu Y., Xiao S., and Zhu X.D. MRE11-RAD50-NBS1 and ATM function as co-mediators of TRF1 in telomere length control. Nature Struct. Mol. Biol. 14 (2007) 832-840
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 832-840
    • Wu, Y.1    Xiao, S.2    Zhu, X.D.3
  • 38
    • 46649111985 scopus 로고    scopus 로고
    • Regulation of telomeric repeat binding factor 1 binding to telomeres by casein kinase 2-mediated phosphorylation
    • Kim M.K., Kang M.R., Nam H.W., Bae Y.S., Kim Y.S., and Chung I.K. Regulation of telomeric repeat binding factor 1 binding to telomeres by casein kinase 2-mediated phosphorylation. J. Biol. Chem. 283 (2008) 14144-14152
    • (2008) J. Biol. Chem. , vol.283 , pp. 14144-14152
    • Kim, M.K.1    Kang, M.R.2    Nam, H.W.3    Bae, Y.S.4    Kim, Y.S.5    Chung, I.K.6
  • 39
    • 34447129654 scopus 로고    scopus 로고
    • The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins
    • Potts P.R., and Yu H. The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins. Nature Struct. Mol. Biol. 14 (2007) 581-590
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 581-590
    • Potts, P.R.1    Yu, H.2
  • 40
    • 16644368073 scopus 로고    scopus 로고
    • Molecular analysis of PinX1 in human hepatocellular carcinoma
    • Oh B.K., Chae K.J., Park C., and Park Y.N. Molecular analysis of PinX1 in human hepatocellular carcinoma. Oncol. Rep. 12 (2004) 861-866
    • (2004) Oncol. Rep. , vol.12 , pp. 861-866
    • Oh, B.K.1    Chae, K.J.2    Park, C.3    Park, Y.N.4


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