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Volumn 27, Issue 26, 2008, Pages 3653-3661

PML enhances the regulation of p53 by CK1 in response to DNA damage

Author keywords

CK1; Mdm2; p53; PML; Threonine 18 phosphorylation

Indexed keywords

CASEIN KINASE I; CASEIN KINASE IDELTA; CASEIN KINASE IEPSILON; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN MDM2; PROTEIN MDMX; PROTEIN P53; THREONINE; ARSENIC TRIOXIDE; MDM2 PROTEIN, HUMAN; NUCLEAR PROTEIN; ORGANOARSENIC DERIVATIVE; OXIDE; PML PROTEIN, HUMAN; TRANSCRIPTION FACTOR; TUMOR PROTEIN; TUMOR SUPPRESSOR PROTEIN;

EID: 45949110751     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/sj.onc.1211036     Document Type: Article
Times cited : (58)

References (30)
  • 1
    • 0034626696 scopus 로고    scopus 로고
    • IC261, a specific inhibitor of the protein kinases casein kinase 1-delta and -epsilon, triggers the mitotic checkpoint and induces p53-dependent postmitotic effects
    • Behrend L, Milne DM, Stöter M, Deppert W, Campbell LE, Meek DW et al. (2000). IC261, a specific inhibitor of the protein kinases casein kinase 1-delta and -epsilon, triggers the mitotic checkpoint and induces p53-dependent postmitotic effects. Oncogene 19: 5303-5313.
    • (2000) Oncogene , vol.19 , pp. 5303-5313
    • Behrend, L.1    Milne, D.M.2    Stöter, M.3    Deppert, W.4    Campbell, L.E.5    Meek, D.W.6
  • 2
    • 0033567340 scopus 로고    scopus 로고
    • Novel phosphorylation sites of human tumour suppressor protein p53 at Ser20 and Thr18 that disrupt the binding of mdm2 (mouse double minute 2) protein are modified in human cancers
    • Craig AL, Burch L, Vojtesek B, Mikutowska J, Thompson A, Hupp TR. (1999). Novel phosphorylation sites of human tumour suppressor protein p53 at Ser20 and Thr18 that disrupt the binding of mdm2 (mouse double minute 2) protein are modified in human cancers. Biochem J 342(Pt 1): 133-141.
    • (1999) Biochem J , vol.342 , Issue.PART 1 , pp. 133-141
    • Craig, A.L.1    Burch, L.2    Vojtesek, B.3    Mikutowska, J.4    Thompson, A.5    Hupp, T.R.6
  • 4
    • 0033429271 scopus 로고    scopus 로고
    • Protein kinase CK1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15
    • Dumaz N, Milne DM, Meek DW. (1999). Protein kinase CK1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15. FEBS Lett 463: 312-316.
    • (1999) FEBS Lett , vol.463 , pp. 312-316
    • Dumaz, N.1    Milne, D.M.2    Meek, D.W.3
  • 6
    • 0027979073 scopus 로고
    • Budding and fission yeast casein kinase I isoforms have dual-specificity protein kinase activity
    • Hoekstra MF, Dhillon N, Carmel G, DeMaggio AJ, Lindberg RA, Hunter T et al. (1994). Budding and fission yeast casein kinase I isoforms have dual-specificity protein kinase activity. Mol Biol Cell 5: 877-886.
    • (1994) Mol Biol Cell , vol.5 , pp. 877-886
    • Hoekstra, M.F.1    Dhillon, N.2    Carmel, G.3    DeMaggio, A.J.4    Lindberg, R.A.5    Hunter, T.6
  • 7
    • 0347716455 scopus 로고    scopus 로고
    • MDM2, an introduction
    • Iwakuma T, Lozano G. (2003). MDM2, an introduction. Mol Cancer Res 1: 993-1000.
    • (2003) Mol Cancer Res , vol.1 , pp. 993-1000
    • Iwakuma, T.1    Lozano, G.2
  • 8
    • 13844294211 scopus 로고    scopus 로고
    • The casein kinase 1 family: Participation in multiple cellular processes in eukaryotes
    • Knippschild U, Gocht A, Wolff S, Huber N, Löhler J, Stöter M. (2005). The casein kinase 1 family: participation in multiple cellular processes in eukaryotes. Cell Signal 17: 675-689.
    • (2005) Cell Signal , vol.17 , pp. 675-689
    • Knippschild, U.1    Gocht, A.2    Wolff, S.3    Huber, N.4    Löhler, J.5    Stöter, M.6
  • 9
    • 0030670332 scopus 로고    scopus 로고
    • p53 is phosphorylated in vitro and in vivo by the delta and epsilon isoforms of casein kinase 1 and enhances the level of casein kinase 1 delta in response to topoisomerase-directed drugs
    • Knippschild U, Milne DM, Campbell LE, DeMaggio AJ, Christenson E, Hoekstra MF et al. (1997). p53 is phosphorylated in vitro and in vivo by the delta and epsilon isoforms of casein kinase 1 and enhances the level of casein kinase 1 delta in response to topoisomerase-directed drugs. Oncogene 15: 1727-1736.
    • (1997) Oncogene , vol.15 , pp. 1727-1736
    • Knippschild, U.1    Milne, D.M.2    Campbell, L.E.3    DeMaggio, A.J.4    Christenson, E.5    Hoekstra, M.F.6
  • 10
    • 0034664684 scopus 로고    scopus 로고
    • Thermodynamics of p53 binding to hdm2 (1-126): Effects of phosphorylation and p53 peptide length
    • Lai Z, Auger KR, Manubay CM, Copeland RA. (2000). Thermodynamics of p53 binding to hdm2 (1-126): effects of phosphorylation and p53 peptide length. Arch Biochem Biophys 381: 278-284.
    • (2000) Arch Biochem Biophys , vol.381 , pp. 278-284
    • Lai, Z.1    Auger, K.R.2    Manubay, C.M.3    Copeland, R.A.4
  • 11
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E, Pearson M, Faretta M, Bauer UM, Frye RA, Minucci S et al. (2002). Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J 21: 2383-2396.
    • (2002) EMBO J , vol.21 , pp. 2383-2396
    • Langley, E.1    Pearson, M.2    Faretta, M.3    Bauer, U.M.4    Frye, R.A.5    Minucci, S.6
  • 12
    • 33646757232 scopus 로고    scopus 로고
    • The complexity of p53 stabilization and activation
    • Lavin MF, Gueven N. (2006). The complexity of p53 stabilization and activation. Cell Death Differ 13: 941-950.
    • (2006) Cell Death Differ , vol.13 , pp. 941-950
    • Lavin, M.F.1    Gueven, N.2
  • 13
    • 0041856232 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation
    • Louria-Hayon I, Grossman T, Sionov RV, Alsheich O, Pandolfi PP, Haupt Y. (2003). The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation. J Biol Chem 278: 33134-33141.
    • (2003) J Biol Chem , vol.278 , pp. 33134-33141
    • Louria-Hayon, I.1    Grossman, T.2    Sionov, R.V.3    Alsheich, O.4    Pandolfi, P.P.5    Haupt, Y.6
  • 15
    • 0041629453 scopus 로고    scopus 로고
    • Casein kinase I delta (CKIdelta)is involved in lymphocyte physiology
    • Maritzen T, Lohler J, Deppert W, Knippschild U. (2003). Casein kinase I delta (CKIdelta)is involved in lymphocyte physiology. Eur J Cell Biol 82: 369-378.
    • (2003) Eur J Cell Biol , vol.82 , pp. 369-378
    • Maritzen, T.1    Lohler, J.2    Deppert, W.3    Knippschild, U.4
  • 17
    • 3242883729 scopus 로고    scopus 로고
    • The p53 response to DNA damage
    • Meek DW. (2004). The p53 response to DNA damage. DNA Repair (Amst) 3: 1049-1056.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 1049-1056
    • Meek, D.W.1
  • 18
    • 0032402135 scopus 로고    scopus 로고
    • Trivalent antimonials induce degradation of the PML-RAR oncoprotein and reorganization of the promyelocytic leukemia nuclear bodies in acute promyelocytic leukemia NB4 cells
    • Muller S, Miller Jr WH, Dejean A. (1998). Trivalent antimonials induce degradation of the PML-RAR oncoprotein and reorganization of the promyelocytic leukemia nuclear bodies in acute promyelocytic leukemia NB4 cells. Blood 92: 4308-4316.
    • (1998) Blood , vol.92 , pp. 4308-4316
    • Muller, S.1    Miller Jr, W.H.2    Dejean, A.3
  • 19
    • 7144264382 scopus 로고    scopus 로고
    • Wt-p53 action in human leukaemia cell lines corresponding to different stages of differentiation
    • Rizzo MG, Zepparoni A, Cristofanelli B, Scardigli R, Crescenzi M, Blandino G et al. (1998). Wt-p53 action in human leukaemia cell lines corresponding to different stages of differentiation. Br J Cancer 77: 1429-1438.
    • (1998) Br J Cancer , vol.77 , pp. 1429-1438
    • Rizzo, M.G.1    Zepparoni, A.2    Cristofanelli, B.3    Scardigli, R.4    Crescenzi, M.5    Blandino, G.6
  • 20
    • 0141733164 scopus 로고    scopus 로고
    • Phosphorylation site interdependence of human p53 post-translational modifications in response to stress
    • Saito S, Yamaguchi H, Higashimoto Y, Chao C, Xu Y, Fornace Jr AJ et al. (2003). Phosphorylation site interdependence of human p53 post-translational modifications in response to stress. J Biol Chem 278: 37536-37544.
    • (2003) J Biol Chem , vol.278 , pp. 37536-37544
    • Saito, S.1    Yamaguchi, H.2    Higashimoto, Y.3    Chao, C.4    Xu, Y.5    Fornace Jr, A.J.6
  • 21
    • 0034737438 scopus 로고    scopus 로고
    • Damage-mediated phosphorylation of human p53 threonine 18 through a cascade mediated by a casein 1-like kinase. Effect on Mdm2 binding
    • Sakaguchi K, Saito S, Higashimoto Y, Roy S, Anderson CW, Appella E. (2000). Damage-mediated phosphorylation of human p53 threonine 18 through a cascade mediated by a casein 1-like kinase. Effect on Mdm2 binding. J Biol Chem 275: 9278-9283.
    • (2000) J Biol Chem , vol.275 , pp. 9278-9283
    • Sakaguchi, K.1    Saito, S.2    Higashimoto, Y.3    Roy, S.4    Anderson, C.W.5    Appella, E.6
  • 22
    • 0036305633 scopus 로고    scopus 로고
    • p53 De-ubiquitination: At the edge between life and death
    • Salomoni P, Pandolfi PP. (2002). p53 De-ubiquitination: at the edge between life and death. Nat Cell Biol 4: E152-E153.
    • (2002) Nat Cell Biol , vol.4
    • Salomoni, P.1    Pandolfi, P.P.2
  • 24
    • 0034898859 scopus 로고    scopus 로고
    • c-Abl regulates p53 levels under normal and stress conditions by preventing its nuclear export and ubiquitination
    • Sionov RV, Coen S, Goldberg Z, Berger M, Bercovich B, Ben-Neriah Y et al. (2001). c-Abl regulates p53 levels under normal and stress conditions by preventing its nuclear export and ubiquitination. Mol Cell Biol 21: 5869-5878.
    • (2001) Mol Cell Biol , vol.21 , pp. 5869-5878
    • Sionov, R.V.1    Coen, S.2    Goldberg, Z.3    Berger, M.4    Bercovich, B.5    Ben-Neriah, Y.6
  • 25
    • 4544368194 scopus 로고    scopus 로고
    • Structured DNA promotes phosphorylation of p53 by DNA-dependent protein kinase at serine 9 and threonine 18
    • Soubeyrand S, Schild-Poulter C, Haché RJ. (2004). Structured DNA promotes phosphorylation of p53 by DNA-dependent protein kinase at serine 9 and threonine 18. Eur J Biochem 271: 3776-3784.
    • (2004) Eur J Biochem , vol.271 , pp. 3776-3784
    • Soubeyrand, S.1    Schild-Poulter, C.2    Haché, R.J.3
  • 28
    • 33750978419 scopus 로고    scopus 로고
    • Casein kinase 1 delta (CK1delta) interacts with the SNARE associated protein snapin
    • Wolff S, Stoter M, Giamas G, Piesche M, Henne-Bruns D, Banting G et al. (2006). Casein kinase 1 delta (CK1delta) interacts with the SNARE associated protein snapin. FEBS Lett 580: 6477-6484.
    • (2006) FEBS Lett , vol.580 , pp. 6477-6484
    • Wolff, S.1    Stoter, M.2    Giamas, G.3    Piesche, M.4    Henne-Bruns, D.5    Banting, G.6
  • 29
    • 0030890942 scopus 로고    scopus 로고
    • Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia
    • Zhu J, Koken MH, Quignon F, Chelbi-Alix MK, Degos L, Wang ZY et al. (1997). Arsenic-induced PML targeting onto nuclear bodies: implications for the treatment of acute promyelocytic leukemia. Proc Natl Acad Sci USA 94: 3978-3983.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3978-3983
    • Zhu, J.1    Koken, M.H.2    Quignon, F.3    Chelbi-Alix, M.K.4    Degos, L.5    Wang, Z.Y.6
  • 30
    • 3142654673 scopus 로고    scopus 로고
    • Nuclear bodies and compartments: Functional roles and cellular signaling in health and disease
    • Zimber A, Nguyen QD, Gespach C. (2004). Nuclear bodies and compartments: functional roles and cellular signaling in health and disease. Cell Signal 16: 1085-1104.
    • (2004) Cell Signal , vol.16 , pp. 1085-1104
    • Zimber, A.1    Nguyen, Q.D.2    Gespach, C.3


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