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Volumn 2, Issue 1, 2011, Pages

Cyclin B-dependent kinase 1 regulates human TRF1 to modulate the resolution of sister telomeres

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN B; CYCLIN DEPENDENT KINASE 1; TELOMERIC REPEAT BINDING FACTOR 1; THREONINE;

EID: 84880307126     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms1372     Document Type: Article
Times cited : (36)

References (43)
  • 1
    • 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, 2100-2110 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 2100-2110
    • De Lange, T.1
  • 2
    • 10944240539 scopus 로고    scopus 로고
    • Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins
    • Liu, D., O'Connor, M. S., Qin, J. & Songyang, Z. Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins. J. Biol. Chem. 279, 51338-51342 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 51338-51342
    • Liu, D.1    O'Connor, M.S.2    Qin, J.3    Songyang, Z.4
  • 3
    • 46249125488 scopus 로고    scopus 로고
    • How shelterin protects Mammalian telomeres
    • Palm, W. & de Lange, T. How shelterin protects Mammalian telomeres. Annu. Rev. Genet. 42, 301-334 (2008).
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 301-334
    • Palm, W.1    De Lange, T.2
  • 4
    • 0347723876 scopus 로고    scopus 로고
    • Importance of TRF1 for functional telomere structure
    • Iwano, T., Tachibana, M., Reth, M. & Shinkai, Y. Importance of TRF1 for functional telomere structure. J. Biol. Chem. 279, 1442-1448 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 1442-1448
    • Iwano, T.1    Tachibana, M.2    Reth, M.3    Shinkai, Y.4
  • 5
    • 69749092744 scopus 로고    scopus 로고
    • Increased telomere fragility and fusions resulting from TRF1 deficiency lead to degenerative pathologies and increased cancer in mice
    • Martinez, P. et al. Increased telomere fragility and fusions resulting from TRF1 deficiency lead to degenerative pathologies and increased cancer in mice. Genes Dev. 23, 2060-2075 (2009).
    • (2009) Genes Dev. , vol.23 , pp. 2060-2075
    • Martinez, P.1
  • 6
    • 68949198783 scopus 로고    scopus 로고
    • TERRA RNA binding to TRF2 facilitates heterochromatin formation and ORC recruitment at telomeres
    • Deng, Z., Norseen, J., Wiedmer, A., Riethman, H. & Lieberman, P. M. TERRA RNA binding to TRF2 facilitates heterochromatin formation and ORC recruitment at telomeres. Mol. Cell 35, 403-413 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 403-413
    • Deng, Z.1    Norseen, J.2    Wiedmer, A.3    Riethman, H.4    Lieberman, P.M.5
  • 7
    • 7044232011 scopus 로고    scopus 로고
    • Homologous recombination generates T-loop-sized deletions at human telomeres
    • Wang, R. C., Smogorzewska, A. & de Lange, T. Homologous recombination generates T-loop-sized deletions at human telomeres. Cell 119, 355-368 (2004).
    • (2004) Cell , vol.119 , pp. 355-368
    • Wang, R.C.1    Smogorzewska, A.2    De Lange, T.3
  • 8
    • 67649635974 scopus 로고    scopus 로고
    • Mammalian telomeres resemble fragile sites and require TRF1 for efficient replication
    • Sfeir, A. et al. Mammalian telomeres resemble fragile sites and require TRF1 for efficient replication. Cell 138, 90-103 (2009).
    • (2009) Cell , vol.138 , pp. 90-103
    • Sfeir, A.1
  • 9
    • 70249132548 scopus 로고    scopus 로고
    • Arginine methylation regulates telomere length and stability
    • Mitchell, T. R., Glenfield, K., Jeyanthan, K. & Zhu, X. D. Arginine methylation regulates telomere length and stability. Mol. Cell. Biol. 29, 4918-4934 (2009).
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 4918-4934
    • Mitchell, T.R.1    Glenfield, K.2    Jeyanthan, K.3    Zhu, X.D.4
  • 10
    • 0032489012 scopus 로고    scopus 로고
    • TRF2 protects human telomeres from end-to-end fusions
    • van Steensel, B., Smogorzewska, A. & de Lange, T. TRF2 protects human telomeres from end-to-end fusions. Cell 92, 401-413 (1998).
    • (1998) Cell , vol.92 , pp. 401-413
    • Van Steensel, B.1    Smogorzewska, A.2    De Lange, T.3
  • 11
    • 22144490491 scopus 로고    scopus 로고
    • DNA processing is not required for ATM-mediated telomere damage response after TRF2 deletion
    • Celli, G. B. & de Lange, T. DNA processing is not required for ATM-mediated telomere damage response after TRF2 deletion. Nat. Cell. Biol. 7, 712-718 (2005).
    • (2005) Nat. Cell. Biol. , vol.7 , pp. 712-718
    • Celli, G.B.1    De Lange, T.2
  • 12
    • 0042420304 scopus 로고    scopus 로고
    • DNA damage foci at dysfunctional telomeres
    • Takai, H., Smogorzewska, A. & de Lange, T. DNA damage foci at dysfunctional telomeres. Curr. Biol. 13, 1549-1556 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 1549-1556
    • Takai, H.1    Smogorzewska, A.2    De Lange, T.3
  • 13
    • 0029586089 scopus 로고
    • A human telomeric protein
    • Chong, L. et al. A human telomeric protein. Science 270, 1663-1667 (1995).
    • (1995) Science , vol.270 , pp. 1663-1667
    • Chong, L.1
  • 14
    • 0041689966 scopus 로고    scopus 로고
    • Targeted deletion reveals an essential function for the telomere length regulator Trf1
    • Karlseder, J. et al. Targeted deletion reveals an essential function for the telomere length regulator Trf1. Mol. Cell. Biol. 23, 6533-6541 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6533-6541
    • Karlseder, J.1
  • 15
    • 0031027618 scopus 로고    scopus 로고
    • Control of telomere length by the human telomeric protein TRF1 [see comments]
    • van Steensel, B. & de Lange, T. Control of telomere length by the human telomeric protein TRF1 [see comments]. Nature 385, 740-743 (1997).
    • (1997) Nature , vol.385 , pp. 740-743
    • Van Steensel, B.1    De Lange, T.2
  • 16
    • 0033961281 scopus 로고    scopus 로고
    • Control of human telomere length by TRF1 and TRF2
    • Smogorzewska, A. et al. Control of human telomere length by TRF1 and TRF2. Mol. Cell Biol. 20, 1659-1668 (2000).
    • (2000) Mol. Cell Biol. , vol.20 , pp. 1659-1668
    • Smogorzewska, A.1
  • 17
    • 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. 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, 3474-3487 (2002).
    • (2002) Mol. Cell Biol. , vol.22 , pp. 3474-3487
    • Ancelin, K.1
  • 18
    • 36549030804 scopus 로고    scopus 로고
    • Protein requirements for sister telomere association in human cells
    • Canudas, S. et al. Protein requirements for sister telomere association in human cells. EMBO J. 26, 4867-4878 (2007).
    • (2007) EMBO J. , vol.26 , pp. 4867-4878
    • Canudas, S.1
  • 19
    • 0036766023 scopus 로고    scopus 로고
    • Replication and/or separation of some human telomeres is delayed beyond S-phase in pre-senescent cells
    • Ofir, R. et al. Replication and/or separation of some human telomeres is delayed beyond S-phase in pre-senescent cells. Chromosoma 111, 147-155 (2002).
    • (2002) Chromosoma , vol.111 , pp. 147-155
    • Ofir, R.1
  • 20
    • 2942580948 scopus 로고    scopus 로고
    • Sister chromatid separation at human telomeric regions
    • Yalon, M., Gal, S., Segev, Y., Selig, S. & Skorecki, K. L. Sister chromatid separation at human telomeric regions. J. Cell Sci. 117, 1961-1970 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 1961-1970
    • Yalon, M.1    Gal, S.2    Segev, Y.3    Selig, S.4    Skorecki, K.L.5
  • 21
    • 1842424729 scopus 로고    scopus 로고
    • Resolution of sister telomere association is required for progression through mitosis
    • Dynek, J. N. & Smith, S. Resolution of sister telomere association is required for progression through mitosis. Science 304, 97-100 (2004).
    • (2004) Science , vol.304 , pp. 97-100
    • Dynek, J.N.1    Smith, S.2
  • 22
    • 0032553473 scopus 로고    scopus 로고
    • Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
    • see comments
    • Smith, S., Giriat, I., Schmitt, A. & de Lange, T. Tankyrase, a poly(ADP-ribose) polymerase at human telomeres (see comments). Science 282, 1484-1487 (1998).
    • (1998) Science , vol.282 , pp. 1484-1487
    • Smith, S.1    Giriat, I.2    Schmitt, A.3    De Lange, T.4
  • 23
    • 0037610123 scopus 로고    scopus 로고
    • TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
    • Chang, W., Dynek, J. N. & Smith, S. TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres. Genes Dev. 17, 1328-1333 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 1328-1333
    • Chang, W.1    Dynek, J.N.2    Smith, S.3
  • 24
    • 33644855565 scopus 로고    scopus 로고
    • The F-box protein FBX4 targets PIN2/TRF1 for ubiquitin-mediated degradation and regulates telomere maintenance
    • Lee, T. H., Perrem, K., Harper, J. W., Lu, K. P. & Zhou, X. Z. The F-box protein FBX4 targets PIN2/TRF1 for ubiquitin-mediated degradation and regulates telomere maintenance. J. Biol. Chem. 281, 759-768 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 759-768
    • Lee, T.H.1    Perrem, K.2    Harper, J.W.3    Lu, K.P.4    Zhou, X.Z.5
  • 25
    • 70449731229 scopus 로고    scopus 로고
    • Differential regulation of telomere and centromere cohesion by the Scc3 homologues SA1 and SA2, respectively, in human cells
    • Canudas, S. & Smith, S. Differential regulation of telomere and centromere cohesion by the Scc3 homologues SA1 and SA2, respectively, in human cells. J. Cell Biol. 187, 165-173 (2009).
    • (2009) J. Cell Biol. , vol.187 , pp. 165-173
    • Canudas, S.1    Smith, S.2
  • 26
    • 0033695002 scopus 로고    scopus 로고
    • Control of mitosis by changes in the subcellular location of cyclin-B1-Cdk1 and Cdc25C
    • Takizawa, C. G. & Morgan, D. O. Control of mitosis by changes in the subcellular location of cyclin-B1-Cdk1 and Cdc25C. Curr. Opin. Cell Biol. 12, 658-665 (2000).
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 658-665
    • Takizawa, C.G.1    Morgan, D.O.2
  • 27
    • 65349102972 scopus 로고    scopus 로고
    • The decision to enter mitosis: Feedback and redundancy in the mitotic entry network
    • Lindqvist, A., Rodriguez-Bravo, V. & Medema, R. H. The decision to enter mitosis: feedback and redundancy in the mitotic entry network. J. Cell Biol. 185, 193-202 (2009).
    • (2009) J. Cell Biol. , vol.185 , pp. 193-202
    • Lindqvist, A.1    Rodriguez-Bravo, V.2    Medema, R.H.3
  • 28
    • 0342561644 scopus 로고    scopus 로고
    • Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres
    • Zhu, X. D., Kuster, B., Mann, M., Petrini, J. H. & Lange, T. Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres. Nat. Genet. 25, 347-352 (2000).
    • (2000) Nat. Genet. , vol.25 , pp. 347-352
    • Zhu, X.D.1    Kuster, B.2    Mann, M.3    Petrini, J.H.4    Lange, T.5
  • 29
    • 54449087207 scopus 로고    scopus 로고
    • Plk1 phosphorylation of TRF1 is essential for its binding to telomeres
    • Wu, Z. Q., Yang, X., Weber, G. & Liu, X. Plk1 phosphorylation of TRF1 is essential for its binding to telomeres. J. Biol. Chem. 283, 25503-25513 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 25503-25513
    • Wu, Z.Q.1    Yang, X.2    Weber, G.3    Liu, X.4
  • 30
    • 0034847376 scopus 로고    scopus 로고
    • Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2
    • Fairall, L., Chapman, L., Moss, H., de Lange, T. & Rhodes, D. Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2. Mol. Cell 8, 351-361 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 351-361
    • Fairall, L.1    Chapman, L.2    Moss, H.3    De Lange, T.4    Rhodes, D.5
  • 31
    • 2642535870 scopus 로고    scopus 로고
    • TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex
    • Ye, J. Z. & de Lange, T. TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex. Nat. Genet. 36, 618-623 (2004).
    • (2004) Nat. Genet. , vol.36 , pp. 618-623
    • Ye, J.Z.1    De Lange, T.2
  • 32
    • 0036032778 scopus 로고    scopus 로고
    • Regulators of serine/threonine protein phosphatases at the dawn of a clinical era?
    • Honkanen, R. E. & Golden, T. Regulators of serine/threonine protein phosphatases at the dawn of a clinical era? Curr. Med. Chem. 9, 2055-2075 (2002).
    • (2002) Curr. Med. Chem. , vol.9 , pp. 2055-2075
    • Honkanen, R.E.1    Golden, T.2
  • 33
    • 77949486429 scopus 로고    scopus 로고
    • p53 Prevents entry into mitosis with uncapped telomeres
    • Thanasoula, M. et al. p53 Prevents entry into mitosis with uncapped telomeres. Curr. Biol. 20, 521-526 (2010).
    • (2010) Curr. Biol. , vol.20 , pp. 521-526
    • Thanasoula, M.1
  • 34
    • 2942587456 scopus 로고    scopus 로고
    • Dynamics of protein binding to telomeres in living cells: Implications for telomere structure and function
    • Mattern, K. A. et al. Dynamics of protein binding to telomeres in living cells: implications for telomere structure and function. Mol. Cell. Biol. 24, 5587-5594 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5587-5594
    • Mattern, K.A.1
  • 35
    • 33846210498 scopus 로고    scopus 로고
    • XPF with mutations in its conserved nuclease domain is defective in DNA repair but functions in TRF2-mediated telomere shortening
    • Wu, Y., Zacal, N. J., Rainbow, A. J. & Zhu, X. D. XPF with mutations in its conserved nuclease domain is defective in DNA repair but functions in TRF2-mediated telomere shortening. DNA. Repair. (Amst) 6, 157-166 (2007).
    • (2007) DNA. Repair. (Amst) , vol.6 , pp. 157-166
    • Wu, Y.1    Zacal, N.J.2    Rainbow, A.J.3    Zhu, X.D.4
  • 36
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of 'parallel' expression vectors
    • Sheffield, P., Garrard, S. & Derewenda, Z. Overcoming expression and purification problems of RhoGDI using a family of 'parallel' expression vectors. Protein Expr. Purif. 15, 34-39 (1999).
    • (1999) Protein Expr. Purif. , vol.15 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3
  • 37
    • 0037192462 scopus 로고    scopus 로고
    • Senescence induced by altered telomere state, not telomere loss
    • Karlseder, J., Smogorzewska, A. & de Lange, T. Senescence induced by altered telomere state, not telomere loss. Science 295, 2446-2449 (2002).
    • (2002) Science , vol.295 , pp. 2446-2449
    • Karlseder, J.1    Smogorzewska, A.2    De Lange, T.3
  • 38
    • 0347416975 scopus 로고    scopus 로고
    • ERCC1/XPF removes the 3′ overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes
    • Zhu, X. D. et al. ERCC1/XPF removes the 3′ overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes. Mol. Cell 12, 1489-1498 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1489-1498
    • Zhu, X.D.1
  • 39
    • 0038451396 scopus 로고    scopus 로고
    • POT1 as a terminal transducer of TRF1 telomere length control
    • Loayza, D. & De Lange, T. POT1 as a terminal transducer of TRF1 telomere length control. Nature 424, 1013-1018 (2003).
    • (2003) Nature , vol.424 , pp. 1013-1018
    • Loayza, D.1    De Lange, T.2
  • 40
    • 34548492016 scopus 로고    scopus 로고
    • MRE11-RAD50-NBS1 and ATM function as co-mediators of TRF1 in telomere length control
    • Wu, Y., Xiao, S. & Zhu, X. D. MRE11-RAD50-NBS1 and ATM function as co-mediators of TRF1 in telomere length control. Nat. Struct. Mol. Biol. 14, 832-840 (2007).
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 832-840
    • Wu, Y.1    Xiao, S.2    Zhu, X.D.3
  • 41
    • 0029939848 scopus 로고    scopus 로고
    • Heterogeneity in telomere length of human chromosomes
    • Lansdorp, P. M. et al. Heterogeneity in telomere length of human chromosomes. Hum. Mol. Genet. 5, 685-691 (1996).
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 685-691
    • Lansdorp, P.M.1
  • 43
    • 54249112218 scopus 로고    scopus 로고
    • Human XPF controls TRF2 and telomere length maintenance through distinctive mechanisms
    • Wu, Y., Mitchell, T. R. & Zhu, X. D. Human XPF controls TRF2 and telomere length maintenance through distinctive mechanisms. Mech. Ageing Dev. 129, 602-610 (2008).
    • (2008) Mech. Ageing Dev. , vol.129 , pp. 602-610
    • Wu, Y.1    Mitchell, T.R.2    Zhu, X.D.3


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