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Volumn 3, Issue 7, 2008, Pages

Tankyrase 1 and tankyrase 2 are essential but redundant for mouse embryonic development

Author keywords

[No Author keywords available]

Indexed keywords

TANKYRASE; TANKYRASE 1; TANKYRASE 2; GLUCOSE; INSULIN; TANKYRASE 2, MOUSE; TANKYRASE-2, MOUSE; TNKS PROTEIN, MOUSE;

EID: 50249090605     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0002639     Document Type: Article
Times cited : (131)

References (30)
  • 2
    • 0032553473 scopus 로고    scopus 로고
    • (l998) Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
    • Smith S, Giriat I, Schmitt A, de Lange T (l998) Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. Science 282: 1484-1487.
    • Science , vol.282 , pp. 1484-1487
    • Smith, S.1    Giriat, I.2    Schmitt, A.3    de Lange, T.4
  • 3
    • 0037200048 scopus 로고    scopus 로고
    • Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner
    • Sbodio JI, Chi NW (2002) Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner. J Biol Chem 277: 31887-31892.
    • (2002) J Biol Chem , vol.277 , pp. 31887-31892
    • Sbodio, J.I.1    Chi, N.W.2
  • 4
    • 0037134452 scopus 로고    scopus 로고
    • The telomeric poly(ADP-ribose) polymerase, tankyrasc 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)
    • Seimiya H, Smith S (2002) The telomeric poly(ADP-ribose) polymerase, tankyrasc 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182). J Biol Chem 277: 14116-14126.
    • (2002) J Biol Chem , vol.277 , pp. 14116-14126
    • Seimiya, H.1    Smith, S.2
  • 5
    • 27444438371 scopus 로고    scopus 로고
    • NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis
    • Chang W, Dynek JN, Smith S (2005) NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis. Biochem J 391: 177-184.
    • (2005) Biochem J , vol.391 , pp. 177-184
    • Chang, W.1    Dynek, J.N.2    Smith, S.3
  • 6
    • 33644774924 scopus 로고    scopus 로고
    • Tankyrase 2 poly(ADP-ribose) polymerase domain-deleted mice exhibit growth defects but have normal telomere length and capping
    • Hsiao SJ, Poitras MF, Cook BD, Liu Y, Smith S (2006) Tankyrase 2 poly(ADP-ribose) polymerase domain-deleted mice exhibit growth defects but have normal telomere length and capping. Mol Cell Biol 26: 2044-2054.
    • (2006) Mol Cell Biol , vol.26 , pp. 2044-2054
    • Hsiao, S.J.1    Poitras, M.F.2    Cook, B.D.3    Liu, Y.4    Smith, S.5
  • 7
    • 14544277627 scopus 로고    scopus 로고
    • Telomeres and telomerase: Their mechanisms of action and the effects of altering their functions
    • Bhackburn EH (2005) Telomeres and telomerase: their mechanisms of action and the effects of altering their functions. FEBS Lett 579: 859-862.
    • (2005) FEBS Lett , vol.579 , pp. 859-862
    • Bhackburn, E.H.1
  • 8
    • 38049019132 scopus 로고    scopus 로고
    • Human diseases of telomerase dysfunction: Insights into tissue aging
    • Garcia CK, Wright WE, Shay JW (2007) Human diseases of telomerase dysfunction: insights into tissue aging. Nucleic Acids Res 35: 7406-7416.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7406-7416
    • Garcia, C.K.1    Wright, W.E.2    Shay, J.W.3
  • 9
    • 33745849998 scopus 로고    scopus 로고
    • The structure and function of telomerase reverse transcriptase
    • Autexier C, Lue NF (2006) The structure and function of telomerase reverse transcriptase. Annu Rev Biochem 75: 493-517.
    • (2006) Annu Rev Biochem , vol.75 , pp. 493-517
    • Autexier, C.1    Lue, N.F.2
  • 10
    • 0036132673 scopus 로고    scopus 로고
    • Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres
    • Cook BD, Dynek JN, Chang W, Shostak G, Smith S (2002) Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres. Mol Cell Biol 22: 332-342.
    • (2002) Mol Cell Biol , vol.22 , pp. 332-342
    • Cook, B.D.1    Dynek, J.N.2    Chang, W.3    Shostak, G.4    Smith, S.5
  • 11
    • 0034687248 scopus 로고    scopus 로고
    • Tankyrase promotes telomere elongation in human cells
    • Smith S, de Lange T (2000) Tankyrase promotes telomere elongation in human cells. Curr Biol 10: 1299-1302.
    • (2000) Curr Biol , vol.10 , pp. 1299-1302
    • Smith, S.1    de Lange, T.2
  • 13
    • 1842424729 scopus 로고    scopus 로고
    • Resolution of sister telomere association is required for progression through mitosis
    • Dynek JN, Smith S (2004) Resolution of sister telomere association is required for progression through mitosis. Science 304: 97-100.
    • (2004) Science , vol.304 , pp. 97-100
    • Dynek, J.N.1    Smith, S.2
  • 14
    • 36549030804 scopus 로고    scopus 로고
    • Protein requirements for sister telomere association in human cells
    • Canudas S, Houghtaling BR, Kim JY, Dynek JN, Chang WG, et al. (2007) Protein requirements for sister telomere association in human cells. Embo J 26: 4867-4878.
    • (2007) Embo J , vol.26 , pp. 4867-4878
    • Canudas, S.1    Houghtaling, B.R.2    Kim, J.Y.3    Dynek, J.N.4    Chang, W.G.5
  • 15
    • 33847701165 scopus 로고    scopus 로고
    • Insulin-stimulated exocytosis of GLUT4 is enhanced by IRAP and its partner tankyrase
    • Yeh TY, Sbodio JI, Tsun ZY, Luo B, Chi NW (2007) Insulin-stimulated exocytosis of GLUT4 is enhanced by IRAP and its partner tankyrase. Biochem J 402: 279-290.
    • (2007) Biochem J , vol.402 , pp. 279-290
    • Yeh, T.Y.1    Sbodio, J.I.2    Tsun, Z.Y.3    Luo, B.4    Chi, N.W.5
  • 16
    • 0034623934 scopus 로고    scopus 로고
    • Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles
    • Chi NWV, Lodish HF (2000) Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles. J Biol Chem 275: 38437-38444.
    • (2000) J Biol Chem , vol.275 , pp. 38437-38444
    • Chi, N.W.V.1    Lodish, H.F.2
  • 17
    • 0036472339 scopus 로고    scopus 로고
    • Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)
    • Sbodio JI, Lodish HF, Chi NW (2002) Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase). Biochem J 361: 451-459.
    • (2002) Biochem J , vol.361 , pp. 451-459
    • Sbodio, J.I.1    Lodish, H.F.2    Chi, N.W.3
  • 18
    • 33644755929 scopus 로고    scopus 로고
    • Generation and characterization of telomere length maintenance in tankyrase 2-deficient mice
    • Chiang YJ, Nguyen ML, Gurunathan S, Kaminker P, Tessarollo L, et al. (2006) Generation and characterization of telomere length maintenance in tankyrase 2-deficient mice. Mol Cell Biol 26: 2037-2043.
    • (2006) Mol Cell Biol , vol.26 , pp. 2037-2043
    • Chiang, Y.J.1    Nguyen, M.L.2    Gurunathan, S.3    Kaminker, P.4    Tessarollo, L.5
  • 19
    • 0035227286 scopus 로고    scopus 로고
    • Gene Knockouts: Manipulating mouse embryonic stem cells
    • Tessarollo L (2001) Gene Knockouts: Manipulating mouse embryonic stem cells. Methods Mol Biol 158: 47-453.
    • (2001) Methods Mol Biol , vol.158 , pp. 47-453
    • Tessarollo, L.1
  • 20
    • 0030008349 scopus 로고    scopus 로고
    • Efficient in vivo manipulation of mouse genomic sequences at the zygote stage
    • Lakso M, Pichel JG, Gorman JR, Sauer B, Okamoto Y, et al. (1996) Efficient in vivo manipulation of mouse genomic sequences at the zygote stage. Proc Natl Acad Sci U S A 93: 5860-5805.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 5860-5805
    • Lakso, M.1    Pichel, J.G.2    Gorman, J.R.3    Sauer, B.4    Okamoto, Y.5
  • 21
    • 0033636363 scopus 로고    scopus 로고
    • Mammalian meiotic telomeres: Protein composition and redistribution in relation to nuclear pores
    • Scherthan H, Jerratsch M, Li B, Smith S, Hulten M, et al. (2000) Mammalian meiotic telomeres: protein composition and redistribution in relation to nuclear pores. Mol Biol Cell 11: 4189-4203.
    • (2000) Mol Biol Cell , vol.11 , pp. 4189-4203
    • Scherthan, H.1    Jerratsch, M.2    Li, B.3    Smith, S.4    Hulten, M.5
  • 22
    • 84925548155 scopus 로고    scopus 로고
    • Telomere length measurement by fluorescence in situ hybridization and flow cytometry: Tips and pitfalls
    • Baerlocher GM, Mak J, Tien T, Lansdorp PM (2002) Telomere length measurement by fluorescence in situ hybridization and flow cytometry: tips and pitfalls. Cytometry 47: 89-99.
    • (2002) Cytometry , vol.47 , pp. 89-99
    • Baerlocher, G.M.1    Mak, J.2    Tien, T.3    Lansdorp, P.M.4
  • 23
    • 27744494860 scopus 로고    scopus 로고
    • Stepwise differentiation of CD4 memory T cells defined by expression of CCR7 and CD27
    • Fritsch RD, Shen X, Sims GP, Hathcock KS, Hodes RJ, et al. (2005) Stepwise differentiation of CD4 memory T cells defined by expression of CCR7 and CD27. J Immunol 175: 6489-6497.
    • (2005) J Immunol , vol.175 , pp. 6489-6497
    • Fritsch, R.D.1    Shen, X.2    Sims, G.P.3    Hathcock, K.S.4    Hodes, R.J.5
  • 24
    • 0021138774 scopus 로고
    • The fate of labelled glucose molecules in the rat adipocyte. Dependence on glucose concentration
    • Gliemann J, Rees WD, Foley JA (1984) The fate of labelled glucose molecules in the rat adipocyte. Dependence on glucose concentration. Biochim Biophys Acta 804: 68-76.
    • (1984) Biochim Biophys Acta , vol.804 , pp. 68-76
    • Gliemann, J.1    Rees, W.D.2    Foley, J.A.3
  • 25
    • 0031885801 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor 2 (FGFR2)-mediated reciprocal regulation loop between FGF8 and FGF10 is essential for limb induction
    • Xu X, Weinstein M, Li C, Naski M, Cohen RI, et al. (1998) Fibroblast growth factor receptor 2 (FGFR2)-mediated reciprocal regulation loop between FGF8 and FGF10 is essential for limb induction. Development 125: 753-765.
    • (1998) Development , vol.125 , pp. 753-765
    • Xu, X.1    Weinstein, M.2    Li, C.3    Naski, M.4    Cohen, R.I.5
  • 26
    • 0037610123 scopus 로고    scopus 로고
    • TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
    • Chang W, Dynek JN, Smith S (2003) TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres. Genes Dev 17: 1328-1333.
    • (2003) Genes Dev , vol.17 , pp. 1328-1333
    • Chang, W.1    Dynek, J.N.2    Smith, S.3
  • 27
    • 0030931491 scopus 로고    scopus 로고
    • Telomere shortening and tumor formation by mouse cells lacking telomerase RNA
    • Blasco MA, Lee HW, Hande MP, Samper E, Lansdorp PM, et al. (1997) Telomere shortening and tumor formation by mouse cells lacking telomerase RNA. Cell 91: 25-34.
    • (1997) Cell , vol.91 , pp. 25-34
    • Blasco, M.A.1    Lee, H.W.2    Hande, M.P.3    Samper, E.4    Lansdorp, P.M.5
  • 28
    • 3543010768 scopus 로고    scopus 로고
    • Expression of telomerase RNA template, but not telomerase reverse transcriptase, is limiting for telomere length maintenance in vivo
    • Chiang YJ, Hemann MT, Hathcock KS, Tessarollo L, Feigenbaum L, et al. (2004) Expression of telomerase RNA template, but not telomerase reverse transcriptase, is limiting for telomere length maintenance in vivo. Mol Cell Biol 24: 7024-7031.
    • (2004) Mol Cell Biol , vol.24 , pp. 7024-7031
    • Chiang, Y.J.1    Hemann, M.T.2    Hathcock, K.S.3    Tessarollo, L.4    Feigenbaum, L.5
  • 29
    • 1942437469 scopus 로고    scopus 로고
    • Distinct dosage requirements for the maintenance of long and short telomeres in mTert heterozygous mice
    • Erdmann N, Liu Y, Harrington L (2004) Distinct dosage requirements for the maintenance of long and short telomeres in mTert heterozygous mice. Proc Natl Acad Sci U S A 101: 6080-6085.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 6080-6085
    • Erdmann, N.1    Liu, Y.2    Harrington, L.3
  • 30
    • 20344368293 scopus 로고    scopus 로고
    • In vivo regulation of telomerase activity and telomere length
    • Hathcock KS, Jeffrey Ghiang Y, Hodes RJ (2005) In vivo regulation of telomerase activity and telomere length. Immunol Rev 205: 104-113.
    • (2005) Immunol Rev , vol.205 , pp. 104-113
    • Hathcock, K.S.1    Jeffrey Ghiang, Y.2    Hodes, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.