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Volumn 15, Issue 1, 2008, Pages 79-84

Pot1 and cell cycle progression cooperate in telomere length regulation

Author keywords

[No Author keywords available]

Indexed keywords

ATR PROTEIN; BINDING PROTEIN; CHECKPOINT KINASE 1; TELOMERE PROTEIN POT1; UNCLASSIFIED DRUG;

EID: 37849030208     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1331     Document Type: Article
Times cited : (57)

References (50)
  • 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
    • 33750033205 scopus 로고    scopus 로고
    • The role of the nonhomologous end-joining DNA double-strand break repair pathway in telomere biology
    • Riha, K., Heacock, M.L. & Shippen, D.E. The role of the nonhomologous end-joining DNA double-strand break repair pathway in telomere biology. Annu. Rev. Genet. 40, 237-277 (2006).
    • (2006) Annu. Rev. Genet , vol.40 , pp. 237-277
    • Riha, K.1    Heacock, M.L.2    Shippen, D.E.3
  • 3
    • 33747051742 scopus 로고    scopus 로고
    • A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly
    • O'Connor, M.S., Safari, A., Xin, H., Liu, D. & Songyang, Z. A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly. Proc. Natl. Acad. Sci. USA 103, 11874-11879 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11874-11879
    • O'Connor, M.S.1    Safari, A.2    Xin, H.3    Liu, D.4    Songyang, Z.5
  • 4
    • 33846691378 scopus 로고    scopus 로고
    • The POT-TTP1 telomere complex is a telomerase processivity factor
    • Wang, F. et al. The POT-TTP1 telomere complex is a telomerase processivity factor. Nature 445, 506-510 (2007).
    • (2007) Nature , vol.445 , pp. 506-510
    • Wang, F.1
  • 5
    • 0344441890 scopus 로고    scopus 로고
    • A DNA damage checkpoint response in telomere-initiated senescence
    • d'Adda di Fagagna, F. et al. A DNA damage checkpoint response in telomere-initiated senescence. Nature 426, 194-198 (2003).
    • (2003) Nature , vol.426 , pp. 194-198
    • d'Adda di Fagagna, F.1
  • 6
    • 2942644725 scopus 로고    scopus 로고
    • The generation of proper constitutive G-tails on yeast telomeres is dependent on the MRX complex
    • Larrivee, M., LeBel, C. & Wellinger, R.J. The generation of proper constitutive G-tails on yeast telomeres is dependent on the MRX complex. Genes Dev. 18, 1391-1396 (2004).
    • (2004) Genes Dev , vol.18 , pp. 1391-1396
    • Larrivee, M.1    LeBel, C.2    Wellinger, R.J.3
  • 7
    • 33845669591 scopus 로고    scopus 로고
    • The telomerase-recruitment domain of the telomere binding protein Cdc13 is regulated by Mec1p/Tel1p-dependent phosphorylation
    • Tseng, S.F., Lin, J.J. & Teng, S.C. The telomerase-recruitment domain of the telomere binding protein Cdc13 is regulated by Mec1p/Tel1p-dependent phosphorylation. Nucleic Acids Res. 34, 6327-6336 (2006).
    • (2006) Nucleic Acids Res , vol.34 , pp. 6327-6336
    • Tseng, S.F.1    Lin, J.J.2    Teng, S.C.3
  • 8
    • 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
  • 9
    • 34250841785 scopus 로고    scopus 로고
    • Replication and protection of telomeres
    • Verdun, R.E. & Karlseder, J. Replication and protection of telomeres. Nature 447, 924-931 (2007).
    • (2007) Nature , vol.447 , pp. 924-931
    • Verdun, R.E.1    Karlseder, J.2
  • 10
    • 34548269900 scopus 로고    scopus 로고
    • Tel1p preferentially associates with short telomeres to stimulate their elongation
    • Hector, R.E. et al. Tel1p preferentially associates with short telomeres to stimulate their elongation. Mol. Cell 27, 851-858 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 851-858
    • Hector, R.E.1
  • 11
    • 27944496124 scopus 로고    scopus 로고
    • Functional human telomeres are recognized as DNA damage in G2 of the cell cycle
    • Verdun, R.E., Crabbe, L., Haggblom, C. & Karlseder, J. Functional human telomeres are recognized as DNA damage in G2 of the cell cycle. Mol. Cell 20, 551-561 (2005).
    • (2005) Mol. Cell , vol.20 , pp. 551-561
    • Verdun, R.E.1    Crabbe, L.2    Haggblom, C.3    Karlseder, J.4
  • 12
    • 33750801681 scopus 로고    scopus 로고
    • The DNA damage machinery and homologous recombination pathway act consecutively to protect human telomeres
    • Verdun, R.E. & Karlseder, J. The DNA damage machinery and homologous recombination pathway act consecutively to protect human telomeres. Cell 127, 709-720 (2006).
    • (2006) Cell , vol.127 , pp. 709-720
    • Verdun, R.E.1    Karlseder, J.2
  • 13
    • 2442511752 scopus 로고    scopus 로고
    • Telomere shortening triggers senescence of human cells through a pathway involving ATM, p53, and p21(CIP1), but not p16(INK4a)
    • Herbig, U., Jobling, W.A., Chen, B.P., Chen, D.J. & Sedivy, J.M. Telomere shortening triggers senescence of human cells through a pathway involving ATM, p53, and p21(CIP1), but not p16(INK4a). Mol. Cell 14, 501-513 (2004).
    • (2004) Mol. Cell , vol.14 , pp. 501-513
    • Herbig, U.1    Jobling, W.A.2    Chen, B.P.3    Chen, D.J.4    Sedivy, J.M.5
  • 14
    • 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
  • 15
    • 0035844082 scopus 로고    scopus 로고
    • Pot1, the putative telomere end-binding protein in fission yeast and humans
    • Baumann, P. & Cech, T.R. Pot1, the putative telomere end-binding protein in fission yeast and humans. Science 292, 1171-1175 (2001).
    • (2001) Science , vol.292 , pp. 1171-1175
    • Baumann, P.1    Cech, T.R.2
  • 16
    • 33745685066 scopus 로고    scopus 로고
    • Recent expansion of the telomeric complex in rodents: Two distinct Pot1 proteins protect mouse telomeres
    • Hockemeyer, D., Daniels, J.P., Takai, H. & de Lange, T. Recent expansion of the telomeric complex in rodents: two distinct Pot1 proteins protect mouse telomeres. Cell 126, 63-77 (2006).
    • (2006) Cell , vol.126 , pp. 63-77
    • Hockemeyer, D.1    Daniels, J.P.2    Takai, H.3    de Lange, T.4
  • 17
    • 33748656958 scopus 로고    scopus 로고
    • Vertebrate Pot1 restricts G-overhang length and prevents activation of a telomeric DNA damage checkpoint but is dispensable for overhang protection
    • Churikov, D., Wei, C. & Price, C.M. Vertebrate Pot1 restricts G-overhang length and prevents activation of a telomeric DNA damage checkpoint but is dispensable for overhang protection. Mol. Cell. Biol. 26, 6971-6982 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , pp. 6971-6982
    • Churikov, D.1    Wei, C.2    Price, C.M.3
  • 18
    • 33745713451 scopus 로고    scopus 로고
    • Pot1 deficiency initiates DNA damage checkpoint activation and aberrant homologous recombination at telomeres
    • Wu, L. et al. Pot1 deficiency initiates DNA damage checkpoint activation and aberrant homologous recombination at telomeres. Cell 126, 49-62 (2006).
    • (2006) Cell , vol.126 , pp. 49-62
    • Wu, L.1
  • 19
    • 34247251276 scopus 로고    scopus 로고
    • Single- and double-stranded DNA: Building a trigger of ATR-mediated DNA damage response
    • Zou, L. Single- and double-stranded DNA: building a trigger of ATR-mediated DNA damage response. Genes Dev. 21, 879-885 (2007).
    • (2007) Genes Dev , vol.21 , pp. 879-885
    • Zou, L.1
  • 20
    • 0032189483 scopus 로고    scopus 로고
    • Inhibition of phosphoinositide 3-kinase related kinases by the radiosensitizing agent wortmannin
    • Sarkaria, J.N. et al. Inhibition of phosphoinositide 3-kinase related kinases by the radiosensitizing agent wortmannin. Cancer Res. 58, 4375-4382 (1998).
    • (1998) Cancer Res , vol.58 , pp. 4375-4382
    • Sarkaria, J.N.1
  • 21
    • 0038418869 scopus 로고    scopus 로고
    • Chk1 and Chk2 kinases in checkpoint control and cancer
    • Bartek, J. & Lukas, J. Chk1 and Chk2 kinases in checkpoint control and cancer. Cancer Cell 3, 421-429 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 421-429
    • Bartek, J.1    Lukas, J.2
  • 22
    • 0037228519 scopus 로고    scopus 로고
    • The protein kinase C inhibitor Go6976 is a potent inhibitor of DNA damage-induced S and G2 cell cycle checkpoints
    • Kohn, E.A., Yoo, C.J. & Eastman, A. The protein kinase C inhibitor Go6976 is a potent inhibitor of DNA damage-induced S and G2 cell cycle checkpoints. Cancer Res. 63, 31-35 (2003).
    • (2003) Cancer Res , vol.63 , pp. 31-35
    • Kohn, E.A.1    Yoo, C.J.2    Eastman, A.3
  • 23
    • 11844300367 scopus 로고    scopus 로고
    • Chk1-dependent S-M checkpoint delay in vertebrate cells is linked to maintenance of viable replication structures
    • Zachos, G., Rainey, M.D. & Gillespie, D.A. Chk1-dependent S-M checkpoint delay in vertebrate cells is linked to maintenance of viable replication structures. Mol. Cell. Biol. 25, 563-574 (2005).
    • (2005) Mol. Cell. Biol , vol.25 , pp. 563-574
    • Zachos, G.1    Rainey, M.D.2    Gillespie, D.A.3
  • 24
    • 33244471768 scopus 로고    scopus 로고
    • MAPKAP kinases - MKs - two's company, three's a crowd
    • Gaestel, M. MAPKAP kinases - MKs - two's company, three's a crowd. Nat. Rev. Mol. Cell Biol. 7, 120-130 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 120-130
    • Gaestel, M.1
  • 25
    • 33846821915 scopus 로고    scopus 로고
    • p53-deficient cells rely on ATM- and ATR-mediated checkpoint signaling through the p38MAPK/MK2 pathway for survival after DNA damage
    • Reinhardt, H.C., Aslanian, A.S., Lees, J.A. & Yaffe, M.B. p53-deficient cells rely on ATM- and ATR-mediated checkpoint signaling through the p38MAPK/MK2 pathway for survival after DNA damage. Cancer Cell 11, 175-189 (2007).
    • (2007) Cancer Cell , vol.11 , pp. 175-189
    • Reinhardt, H.C.1    Aslanian, A.S.2    Lees, J.A.3    Yaffe, M.B.4
  • 26
    • 30344463835 scopus 로고    scopus 로고
    • ATM- and cell cycle-dependent regulation of ATR in response to DNA double-strand breaks
    • Jazayeri, A. et al. ATM- and cell cycle-dependent regulation of ATR in response to DNA double-strand breaks. Nat. Cell Biol. 8, 37-45 (2006).
    • (2006) Nat. Cell Biol , vol.8 , pp. 37-45
    • Jazayeri, A.1
  • 27
    • 0033604444 scopus 로고    scopus 로고
    • Disruption of ATM in p53-null cells causes multiple functional abnormalities in cellular response to ionizing radiation
    • Takao, N. et al. Disruption of ATM in p53-null cells causes multiple functional abnormalities in cellular response to ionizing radiation. Oncogene 18, 7002-7009 (1999).
    • (1999) Oncogene , vol.18 , pp. 7002-7009
    • Takao, N.1
  • 28
    • 6344285329 scopus 로고    scopus 로고
    • Centrosome amplification induced by DNA damage occurs during a prolonged G2 phase and involves ATM
    • Dodson, H. et al. Centrosome amplification induced by DNA damage occurs during a prolonged G2 phase and involves ATM. EMBO J. 23, 3864-3873 (2004).
    • (2004) EMBO J , vol.23 , pp. 3864-3873
    • Dodson, H.1
  • 29
    • 3242879828 scopus 로고    scopus 로고
    • 1 in the DNA damage response: Conserved roles from yeasts to mammals
    • Chen, Y.S. & Chk, Y. 1 in the DNA damage response: conserved roles from yeasts to mammals. DNA Repair (Amst.) 3, 1025-1032 (2004).
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 1025-1032
    • Chen, Y.S.1    Chk, Y.2
  • 30
    • 0036639851 scopus 로고    scopus 로고
    • Effects of double-strand break repair proteins on vertebrate telomere structure
    • Wei, C., Skopp, R., Takata, M., Takeda, S. & Price, C.M. Effects of double-strand break repair proteins on vertebrate telomere structure. Nucleic Acids Res. 30, 2862-2870 (2002).
    • (2002) Nucleic Acids Res , vol.30 , pp. 2862-2870
    • Wei, C.1    Skopp, R.2    Takata, M.3    Takeda, S.4    Price, C.M.5
  • 31
    • 0032727616 scopus 로고    scopus 로고
    • TIN2, a new regulator of telomere length in human cells
    • Kim, S.H., Kaminker, P. & Campisi, J. TIN2, a new regulator of telomere length in human cells. Nat. Genet. 23, 405-412 (1999).
    • (1999) Nat. Genet , vol.23 , pp. 405-412
    • Kim, S.H.1    Kaminker, P.2    Campisi, J.3
  • 32
    • 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 423, 1013-1018 (2003).
    • (2003) Nature , vol.423 , pp. 1013-1018
    • Loayza, D.1    De Lange, T.2
  • 33
    • 0034687248 scopus 로고    scopus 로고
    • Tankyrase promotes telomere elongation in human cells
    • Smith, S. & de Lange, T. Tankyrase promotes telomere elongation in human cells. Curr. Biol. 10, 1299-1302 (2000).
    • (2000) Curr. Biol , vol.10 , pp. 1299-1302
    • Smith, S.1    de Lange, T.2
  • 34
    • 0344875481 scopus 로고    scopus 로고
    • Rap1 affects the length and heterogeneity of human telomeres
    • Li, B. & De Lange, T. Rap1 affects the length and heterogeneity of human telomeres. Mol. Biol. Cell 14, 5060-5068 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 5060-5068
    • Li, B.1    De Lange, T.2
  • 35
    • 3142679378 scopus 로고    scopus 로고
    • POT1-interacting protein PIP1: A telomere length regulator that recruits POT1 to the TIN2/TRF1 complex
    • Ye, J.Z. et al. POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex. Genes Dev. 18, 1649-1654 (2004).
    • (2004) Genes Dev , vol.18 , pp. 1649-1654
    • Ye, J.Z.1
  • 36
    • 3242680818 scopus 로고    scopus 로고
    • PTOP interacts with POT1 and regulates its localization to telomeres
    • Liu, D. et al. PTOP interacts with POT1 and regulates its localization to telomeres. Nat. Cell Biol. 6, 673-680 (2004).
    • (2004) Nat. Cell Biol , vol.6 , pp. 673-680
    • Liu, D.1
  • 37
    • 0031027618 scopus 로고    scopus 로고
    • Control of telomere length by the human telomeric protein TRF1
    • van Steensel, B. & de Lange, T. Control of telomere length by the human telomeric protein TRF1. Nature 385, 740-743 (1997).
    • (1997) Nature , vol.385 , pp. 740-743
    • van Steensel, B.1    de Lange, T.2
  • 38
    • 33847243648 scopus 로고    scopus 로고
    • Tetrahymena Pot1a regulates telomere length and prevents activation of a cell cycle checkpoint
    • Jacob, N.K., Lescasse, R., Linger, B.R. & Price, C.M. Tetrahymena Pot1a regulates telomere length and prevents activation of a cell cycle checkpoint. Mol Cell Biol 27, 1592-1601 (2007).
    • (2007) Mol Cell Biol , vol.27 , pp. 1592-1601
    • Jacob, N.K.1    Lescasse, R.2    Linger, B.R.3    Price, C.M.4
  • 39
    • 33749626550 scopus 로고    scopus 로고
    • Phosphorylation of Chk1 by ATR is antagonized by a Chk1-regulated protein phosphatase 2A circuit
    • Leung-Pineda, V., Ryan, C.E. & Piwnica-Worms, H. Phosphorylation of Chk1 by ATR is antagonized by a Chk1-regulated protein phosphatase 2A circuit. Mol. Cell. Biol. 26, 7529-7538 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , pp. 7529-7538
    • Leung-Pineda, V.1    Ryan, C.E.2    Piwnica-Worms, H.3
  • 40
    • 20144382152 scopus 로고    scopus 로고
    • Switching human telomerase on and off with hPOT1 protein in vitro
    • Lei, M., Zaug, A.J., Podell, E.R. & Cech, T.R. Switching human telomerase on and off with hPOT1 protein in vitro. J. Biol. Chem. 280, 20449-20456 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 20449-20456
    • Lei, M.1    Zaug, A.J.2    Podell, E.R.3    Cech, T.R.4
  • 41
    • 11844280894 scopus 로고    scopus 로고
    • Human protection of telomeres 1 (POT1) is a negative regulator of telomerase activity in vitro
    • Kelleher, C., Kurth, I. & Lingner, J. Human protection of telomeres 1 (POT1) is a negative regulator of telomerase activity in vitro. Mol. Cell. Biol. 25, 808-818 (2005).
    • (2005) Mol. Cell. Biol , vol.25 , pp. 808-818
    • Kelleher, C.1    Kurth, I.2    Lingner, J.3
  • 42
    • 23044500389 scopus 로고    scopus 로고
    • POT1 protects telomeres from a transient DNA damage response and determines how human chromosomes end
    • Hockemeyer, D., Sfeir, A.J., Shay, J.W., Wright, W.E. & de Lange, T. POT1 protects telomeres from a transient DNA damage response and determines how human chromosomes end. EMBO J. 24, 2667-2678 (2005).
    • (2005) EMBO J , vol.24 , pp. 2667-2678
    • Hockemeyer, D.1    Sfeir, A.J.2    Shay, J.W.3    Wright, W.E.4    de Lange, T.5
  • 43
    • 34548317418 scopus 로고    scopus 로고
    • Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1
    • Denchi, E.L. & de Lange, T. Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1. Nature 448, 1068-1071 (2007).
    • (2007) Nature , vol.448 , pp. 1068-1071
    • Denchi, E.L.1    de Lange, T.2
  • 44
    • 1342282906 scopus 로고    scopus 로고
    • Cell cycle localization, dimerization, and binding domain architecture of the telomere protein cPot1
    • Wei, C. & Price, C.M. Cell cycle localization, dimerization, and binding domain architecture of the telomere protein cPot1. Mol. Cell. Biol. 24, 2091-2102 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 2091-2102
    • Wei, C.1    Price, C.M.2
  • 45
    • 34548243751 scopus 로고    scopus 로고
    • Clamping the Mec1/ATR checkpoint kinase into action
    • Majka, J.N. & Burgers, P.M. Clamping the Mec1/ATR checkpoint kinase into action. Cell Cycle 6, 1157-1160 (2007).
    • (2007) Cell Cycle , vol.6 , pp. 1157-1160
    • Majka, J.N.1    Burgers, P.M.2
  • 46
    • 19344374569 scopus 로고    scopus 로고
    • The telomeric protein TRF2 binds the ATM kinase and can inhibit the ATM-dependent DNA damage response
    • Karlseder, J. et al. The telomeric protein TRF2 binds the ATM kinase and can inhibit the ATM-dependent DNA damage response. PLoS Biol. 2, E240 (2004).
    • (2004) PLoS Biol , vol.2
    • Karlseder, J.1
  • 47
    • 2042429168 scopus 로고    scopus 로고
    • Regulation of telomerase by telomeric proteins
    • Smogorzewska, A. & de Lange, T. Regulation of telomerase by telomeric proteins. Annu. Rev. Biochem. 73, 177-208 (2004).
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 177-208
    • Smogorzewska, A.1    de Lange, T.2
  • 48
    • 33846692105 scopus 로고    scopus 로고
    • TPP1 is a homolog of ciliate TEBP-beta and interacts with POT1 to recruit telomerase
    • Xin, H. et al. TPP1 is a homolog of ciliate TEBP-beta and interacts with POT1 to recruit telomerase. Nature 445, 559-562 (2007).
    • (2007) Nature , vol.445 , pp. 559-562
    • Xin, H.1
  • 49
    • 33750431337 scopus 로고    scopus 로고
    • Regulation of telomere elongation by the cyclin-dependent kinase CDK1
    • Frank, C.J., Hyde, M. & Greider, C.W. Regulation of telomere elongation by the cyclin-dependent kinase CDK1. Mol. Cell 24, 423-432 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 423-432
    • Frank, C.J.1    Hyde, M.2    Greider, C.W.3
  • 50
    • 33749059184 scopus 로고    scopus 로고
    • DNA degradation at unprotected telomeres in yeast is regulated by the CDK1 (Cdc28/Clb) cell-cycle kinase
    • Vodenicharov, M.D. & Wellinger, R.J. DNA degradation at unprotected telomeres in yeast is regulated by the CDK1 (Cdc28/Clb) cell-cycle kinase. Mol. Cell 24, 127-137 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 127-137
    • Vodenicharov, M.D.1    Wellinger, R.J.2


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