메뉴 건너뛰기




Volumn 50, Issue 7, 2017, Pages 373-378

Phosphorylation of p53 at threonine 155 is required for Jab1-mediated nuclear export of p53

Author keywords

COP9 signalosome; Curcumin; Hdm2; Jab1; P53

Indexed keywords

COP9 SIGNALOSOME; COPS5 PROTEIN, HUMAN; PEPTIDE HYDROLASE; PROTEIN P53; SIGNAL PEPTIDE; THREONINE;

EID: 85026471330     PISSN: 19766696     EISSN: 1976670X     Source Type: Journal    
DOI: 10.5483/BMBRep.2017.50.7.077     Document Type: Article
Times cited : (17)

References (35)
  • 1
    • 13944270339 scopus 로고    scopus 로고
    • Senescent cells, tumor suppression, and organismal aging: good citizens, bad neighbors
    • Campisi J (2005) Senescent cells, tumor suppression, and organismal aging: good citizens, bad neighbors. Cell 120, 513-522
    • (2005) Cell , vol.120 , pp. 513-522
    • Campisi, J.1
  • 2
    • 0027109075 scopus 로고
    • Cancer p53, guardian of the genome
    • Lane DP (1992) Cancer. p53, guardian of the genome. Nature 358, 15-16
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 3
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine AJ (1997) p53, the cellular gatekeeper for growth and division. Cell 88, 323-331
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 4
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: the cell's response to p53
    • Vousden KH and Lu X (2002) Live or let die: the cell's response to p53. Nat Rev Cancer 2, 594-604
    • (2002) Nat Rev Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 5
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A and Oren M (1997) Mdm2 promotes the rapid degradation of p53. Nature 387, 296-299
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 6
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat MH, Jones SN and Vousden KH (1997) Regulation of p53 stability by Mdm2. Nature 387, 299-303
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 8
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
    • Roth J, Dobbelstein M, Freedman DA, Shenk T and Levine AJ (1998) Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J 17, 554-564
    • (1998) EMBO J , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 9
    • 0032993486 scopus 로고    scopus 로고
    • Making sense of the COP9 signalosome. A regulatory protein complex conserved from Arabidopsis to human
    • Wei N and Deng XW (1999) Making sense of the COP9 signalosome. A regulatory protein complex conserved from Arabidopsis to human. Trends Genet 15, 98-103
    • (1999) Trends Genet , vol.15 , pp. 98-103
    • Wei, N.1    Deng, X.W.2
  • 10
    • 0037127256 scopus 로고    scopus 로고
    • The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex
    • Tomoda K, Kubota Y, Arata Y et al (2002) The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex. J Biol Chem 277, 2302-2310
    • (2002) J Biol Chem , vol.277 , pp. 2302-2310
    • Tomoda, K.1    Kubota, Y.2    Arata, Y.3
  • 11
    • 0038329328 scopus 로고    scopus 로고
    • The COP9 signalosome promotes degradation of Cyclin E during early Drosophila oogenesis
    • Doronkin S, Djagaeva I and Beckendorf SK (2003) The COP9 signalosome promotes degradation of Cyclin E during early Drosophila oogenesis. Dev Cell 4, 699-710
    • (2003) Dev Cell , vol.4 , pp. 699-710
    • Doronkin, S.1    Djagaeva, I.2    Beckendorf, S.K.3
  • 12
    • 1542314268 scopus 로고    scopus 로고
    • Jab1/CSN5, a component of the COP9 signalosome, regulates transforming growth factor beta signaling by binding to Smad7 and promoting its degradation
    • Kim BC, Lee HJ, Park SH et al (2004) Jab1/CSN5, a component of the COP9 signalosome, regulates transforming growth factor beta signaling by binding to Smad7 and promoting its degradation. Mol Cell Biol 24, 2251-2262
    • (2004) Mol Cell Biol , vol.24 , pp. 2251-2262
    • Kim, B.C.1    Lee, H.J.2    Park, S.H.3
  • 13
    • 18944391961 scopus 로고    scopus 로고
    • CSN5/Jab1 is involved in ligand-dependent degradation of estrogen receptor (alpha) by the proteasome
    • Callige M, Kieffer I and Richard-Foy H (2005) CSN5/Jab1 is involved in ligand-dependent degradation of estrogen receptor (alpha) by the proteasome. Mol Cell Biol 25, 4349-4358
    • (2005) Mol Cell Biol , vol.25 , pp. 4349-4358
    • Callige, M.1    Kieffer, I.2    Richard-Foy, H.3
  • 14
    • 33847689863 scopus 로고    scopus 로고
    • Jab1 as a mediator of nuclear export and cytoplasmic degradation of p53
    • Lee EW, Oh W and Song J (2006) Jab1 as a mediator of nuclear export and cytoplasmic degradation of p53. Mol Cells 22, 133-140
    • (2006) Mol Cells , vol.22 , pp. 133-140
    • Lee, E.W.1    Oh, W.2    Song, J.3
  • 15
    • 33745218066 scopus 로고    scopus 로고
    • Jab1 induces the cytoplasmic localization and degradation of p53 in coordination with Hdm2
    • Oh W, Lee EW, Sung YH et al (2006) Jab1 induces the cytoplasmic localization and degradation of p53 in coordination with Hdm2. J Biol Chem 281, 17457-17465
    • (2006) J Biol Chem , vol.281 , pp. 17457-17465
    • Oh, W.1    Lee, E.W.2    Sung, Y.H.3
  • 16
    • 33749559162 scopus 로고    scopus 로고
    • Jab1 mediates cytoplasmic localization and degradation of West Nile virus capsid protein
    • Oh W, Yang MR, Lee EW et al (2006) Jab1 mediates cytoplasmic localization and degradation of West Nile virus capsid protein. J Biol Chem 281, 30166-30174
    • (2006) J Biol Chem , vol.281 , pp. 30166-30174
    • Oh, W.1    Yang, M.R.2    Lee, E.W.3
  • 17
    • 66749137635 scopus 로고    scopus 로고
    • Jab1/CSN5 induces the cytoplasmic localization and degradation of RUNX3
    • Kim JH, Choi JK, Cinghu S et al (2009) Jab1/CSN5 induces the cytoplasmic localization and degradation of RUNX3. J Cell Biochem 107, 557-565
    • (2009) J Cell Biochem , vol.107 , pp. 557-565
    • Kim, J.H.1    Choi, J.K.2    Cinghu, S.3
  • 18
    • 84954289081 scopus 로고    scopus 로고
    • Down-regulation of the cyclin-dependent kinase inhibitor p57 is mediated by Jab1/Csn5 in hepatocarcinogenesis
    • Guo H, Jing L, Cheng Y et al (2016) Down-regulation of the cyclin-dependent kinase inhibitor p57 is mediated by Jab1/Csn5 in hepatocarcinogenesis. Hepatology 63, 898-913
    • (2016) Hepatology , vol.63 , pp. 898-913
    • Guo, H.1    Jing, L.2    Cheng, Y.3
  • 19
    • 84977518373 scopus 로고    scopus 로고
    • COPS5 amplification and overexpression confers tamoxifen-resistance in ERalphapositive breast cancer by degradation of NCoR
    • Lu R, Hu X, Zhou J et al (2016) COPS5 amplification and overexpression confers tamoxifen-resistance in ERalphapositive breast cancer by degradation of NCoR. Nat Commun 7, 12044
    • (2016) Nat Commun , vol.7 , pp. 12044
    • Lu, R.1    Hu, X.2    Zhou, J.3
  • 20
    • 5644256911 scopus 로고    scopus 로고
    • Multiple functions of Jab1 are required for early embryonic development and growth potential in mice
    • Tomoda K, Yoneda-Kato N, Fukumoto A, Yamanaka S and Kato JY (2004) Multiple functions of Jab1 are required for early embryonic development and growth potential in mice. J Biol Chem 279, 43013-43018
    • (2004) J Biol Chem , vol.279 , pp. 43013-43018
    • Tomoda, K.1    Yoneda-Kato, N.2    Fukumoto, A.3    Yamanaka, S.4    Kato, J.Y.5
  • 21
    • 0035794541 scopus 로고    scopus 로고
    • COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system
    • Bech-Otschir D, Kraft R, Huang X et al (2001) COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. EMBO J 20, 1630-1639
    • (2001) EMBO J , vol.20 , pp. 1630-1639
    • Bech-Otschir, D.1    Kraft, R.2    Huang, X.3
  • 22
    • 33749160125 scopus 로고    scopus 로고
    • Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
    • Yang WH, Kim JE, Nam HW et al (2006) Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability. Nat Cell Biol 8, 1074-1083
    • (2006) Nat Cell Biol , vol.8 , pp. 1074-1083
    • Yang, W.H.1    Kim, J.E.2    Nam, H.W.3
  • 23
    • 0033559256 scopus 로고    scopus 로고
    • A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking
    • Stommel JM, Marchenko ND, Jimenez GS, Moll UM, Hope TJ and Wahl GM (1999) A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking. EMBO J 18, 1660-1672
    • (1999) EMBO J , vol.18 , pp. 1660-1672
    • Stommel, J.M.1    Marchenko, N.D.2    Jimenez, G.S.3    Moll, U.M.4    Hope, T.J.5    Wahl, G.M.6
  • 24
    • 34047103990 scopus 로고    scopus 로고
    • C-terminal modifications regulate MDM2 dissociation and nuclear export of p53
    • Carter S, Bischof O, Dejean A and Vousden KH (2007) C-terminal modifications regulate MDM2 dissociation and nuclear export of p53. Nat Cell Biol 9, 428-435
    • (2007) Nat Cell Biol , vol.9 , pp. 428-435
    • Carter, S.1    Bischof, O.2    Dejean, A.3    Vousden, K.H.4
  • 26
    • 0348134742 scopus 로고    scopus 로고
    • Mono-versus polyubiquitination: differential control of p53 fate by Mdm2
    • Li M, Brooks CL, Wu-Baer F, Chen D, Baer R and Gu W (2003) Mono-versus polyubiquitination: differential control of p53 fate by Mdm2. Science 302, 1972-1975
    • (2003) Science , vol.302 , pp. 1972-1975
    • Li, M.1    Brooks, C.L.2    Wu-Baer, F.3    Chen, D.4    Baer, R.5    Gu, W.6
  • 28
    • 0034282102 scopus 로고    scopus 로고
    • An intact HDM2 RING-finger domain is required for nuclear exclusion of p53
    • Boyd SD, Tsai KY and Jacks T (2000) An intact HDM2 RING-finger domain is required for nuclear exclusion of p53. Nat Cell Biol 2, 563-568
    • (2000) Nat Cell Biol , vol.2 , pp. 563-568
    • Boyd, S.D.1    Tsai, K.Y.2    Jacks, T.3
  • 29
    • 0034282220 scopus 로고    scopus 로고
    • The MDM2 RING-finger domain is required to promote p53 nuclear export
    • Geyer RK, Yu ZK and Maki CG (2000) The MDM2 RING-finger domain is required to promote p53 nuclear export. Nat Cell Biol 2, 569-573
    • (2000) Nat Cell Biol , vol.2 , pp. 569-573
    • Geyer, R.K.1    Yu, Z.K.2    Maki, C.G.3
  • 30
    • 78049302116 scopus 로고    scopus 로고
    • p53 post-translational modification: deregulated in tumorigenesis
    • Dai C and Gu W (2010) p53 post-translational modification: deregulated in tumorigenesis. Trends Mol Med 16, 528-536
    • (2010) Trends Mol Med , vol.16 , pp. 528-536
    • Dai, C.1    Gu, W.2
  • 31
    • 55949083781 scopus 로고    scopus 로고
    • Inhibition of Thr-55 phosphorylation restores p53 nuclear localization and sensitizes cancer cells to DNA damage
    • Cai X and Liu X (2008) Inhibition of Thr-55 phosphorylation restores p53 nuclear localization and sensitizes cancer cells to DNA damage. Proc Natl Acad Sci U S A 105, 16958-16963
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 16958-16963
    • Cai, X.1    Liu, X.2
  • 32
    • 31544457877 scopus 로고    scopus 로고
    • p53 ubiquitination: Mdm2 and beyond
    • Brooks CL and Gu W (2006) p53 ubiquitination: Mdm2 and beyond. Mol Cell 21, 307-315
    • (2006) Mol Cell , vol.21 , pp. 307-315
    • Brooks, C.L.1    Gu, W.2
  • 33
    • 67651154117 scopus 로고    scopus 로고
    • Differential regulation of p53 and p21 by MKRN1 E3 ligase controls cell cycle arrest and apoptosis
    • Lee EW, Lee MS, Camus S et al (2009) Differential regulation of p53 and p21 by MKRN1 E3 ligase controls cell cycle arrest and apoptosis. EMBO J 28, 2100-2113
    • (2009) EMBO J , vol.28 , pp. 2100-2113
    • Lee, E.W.1    Lee, M.S.2    Camus, S.3
  • 34
    • 84959241995 scopus 로고    scopus 로고
    • CHIP controls necroptosis through ubiquitylation-and lysosomedependent degradation of RIPK3
    • Seo J, Lee EW, Sung H et al (2016) CHIP controls necroptosis through ubiquitylation-and lysosomedependent degradation of RIPK3. Nat Cell Biol 18, 291-302
    • (2016) Nat Cell Biol , vol.18 , pp. 291-302
    • Seo, J.1    Lee, E.W.2    Sung, H.3
  • 35
    • 84864857213 scopus 로고    scopus 로고
    • Ubiquitination and degradation of the FADD adaptor protein regulate death receptor-mediated apoptosis and necroptosis
    • Lee EW, Kim JH, Ahn YH et al (2012) Ubiquitination and degradation of the FADD adaptor protein regulate death receptor-mediated apoptosis and necroptosis. Nat Commun 3, 978
    • (2012) Nat Commun , vol.3 , pp. 978
    • Lee, E.W.1    Kim, J.H.2    Ahn, Y.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.