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Volumn 8, Issue 10, 2013, Pages

OTUD5 Regulates p53 Stability by Deubiquitinating p53

Author keywords

[No Author keywords available]

Indexed keywords

OTUD5 PROTEIN; PROTEIN P53; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84885452884     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0077682     Document Type: Article
Times cited : (50)

References (27)
  • 1
    • 33847271089 scopus 로고    scopus 로고
    • Coping with stress: multiple ways to activate p53
    • doi:10.1038/sj.onc.1210263
    • Horn HF, Vousden KH, (2007) Coping with stress: multiple ways to activate p53. Oncogene 26: 1306-1316. doi:10.1038/sj.onc.1210263. PubMed: 17322916.
    • (2007) Oncogene , vol.26 , pp. 1306-1316
    • Horn, H.F.1    Vousden, K.H.2
  • 2
    • 33947534030 scopus 로고    scopus 로고
    • p53 in health and disease
    • doi:10.1038/nrm2147
    • Vousden KH, Lane DP, (2007) p53 in health and disease. Nat Rev Mol Cell Biol 8: 275-283. doi:10.1038/nrm2147. PubMed: 17380161.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 275-283
    • Vousden, K.H.1    Lane, D.P.2
  • 3
    • 65549120715 scopus 로고    scopus 로고
    • Modes of p53 regulation
    • doi:10.1016/j.cell.2009.04.050
    • Kruse JP, Gu W, (2009) Modes of p53 regulation. Cell 137: 609-622. doi:10.1016/j.cell.2009.04.050. PubMed: 19450511.
    • (2009) Cell , vol.137 , pp. 609-622
    • Kruse, J.P.1    Gu, W.2
  • 4
    • 84861973567 scopus 로고    scopus 로고
    • Tumor suppression in the absence of p53-mediated cell-cycle arrest, apoptosis, and senescence
    • doi:10.1016/j.cell.2012.04.026
    • Li T, Kon N, Jiang L, Tan M, Ludwig T, et al. (2012) Tumor suppression in the absence of p53-mediated cell-cycle arrest, apoptosis, and senescence. Cell 149: 1269-1283. doi:10.1016/j.cell.2012.04.026. PubMed: 22682249.
    • (2012) Cell , vol.149 , pp. 1269-1283
    • Li, T.1    Kon, N.2    Jiang, L.3    Tan, M.4    Ludwig, T.5
  • 5
    • 28344456279 scopus 로고    scopus 로고
    • A genomic and functional inventory of deubiquitinating enzymes
    • doi:10.1016/j.cell.2005.11.007
    • Nijman SM, Luna-Vargas MP, Velds A, Brummelkamp TR, Dirac AM, et al. (2005) A genomic and functional inventory of deubiquitinating enzymes. Cell 123: 773-786. doi:10.1016/j.cell.2005.11.007. PubMed: 16325574.
    • (2005) Cell , vol.123 , pp. 773-786
    • Nijman, S.M.1    Luna-Vargas, M.P.2    Velds, A.3    Brummelkamp, T.R.4    Dirac, A.M.5
  • 6
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: structure and function of the deubiquitinases
    • doi:10.1038/nrm2731
    • Komander D, Clague MJ, Urbé S, (2009) Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 10: 550-563. doi:10.1038/nrm2731. PubMed: 19626045.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbé, S.3
  • 7
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • doi:10.1016/S1097-2765(04)00157-1
    • Li M, Brooks CL, Kon N, Gu W, (2004) A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol Cell 13: 879-886. doi:10.1016/S1097-2765(04)00157-1. PubMed: 15053880.
    • (2004) Mol Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 8
    • 3242774545 scopus 로고    scopus 로고
    • HAUSP is required for p53 destabilization
    • Cummins JM, Vogelstein B, (2004) HAUSP is required for p53 destabilization. Cell Cycle 3: 689-692. PubMed: 15118411.
    • (2004) Cell Cycle , vol.3 , pp. 689-692
    • Cummins, J.M.1    Vogelstein, B.2
  • 9
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • doi:10.1038/nature737
    • Li M, Chen D, Shiloh A, Luo J, Nikolaev AY, et al. (2002) Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 416: 648-653. doi:10.1038/nature737. PubMed: 11923872.
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5
  • 10
    • 19444367393 scopus 로고    scopus 로고
    • Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2
    • doi:10.1016/j.molcel.2005.04.024
    • Meulmeester E, Maurice MM, Boutell C, Teunisse AF, Ovaa H, et al. (2005) Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2. Mol Cell 18: 565-576. doi:10.1016/j.molcel.2005.04.024. PubMed: 15916963.
    • (2005) Mol Cell , vol.18 , pp. 565-576
    • Meulmeester, E.1    Maurice, M.M.2    Boutell, C.3    Teunisse, A.F.4    Ovaa, H.5
  • 11
    • 75749132016 scopus 로고    scopus 로고
    • USP10 regulates p53 localization and stability by deubiquitinating p53
    • doi:10.1016/j.cell.2009.12.032
    • Yuan J, Luo K, Zhang L, Cheville JC, Lou Z, (2010) USP10 regulates p53 localization and stability by deubiquitinating p53. Cell 140: 384-396. doi:10.1016/j.cell.2009.12.032. PubMed: 20096447.
    • (2010) Cell , vol.140 , pp. 384-396
    • Yuan, J.1    Luo, K.2    Zhang, L.3    Cheville, J.C.4    Lou, Z.5
  • 12
    • 79952282523 scopus 로고    scopus 로고
    • JTV1 co-activates FBP to induce USP29 transcription and stabilize p53 in response to oxidative stress
    • doi:10.1038/emboj.2011.11
    • Liu J, Chung HJ, Vogt M, Jin Y, Malide D, et al. (2011) JTV1 co-activates FBP to induce USP29 transcription and stabilize p53 in response to oxidative stress. EMBO J 30: 846-858. doi:10.1038/emboj.2011.11. PubMed: 21285945.
    • (2011) EMBO J , vol.30 , pp. 846-858
    • Liu, J.1    Chung, H.J.2    Vogt, M.3    Jin, Y.4    Malide, D.5
  • 13
    • 33847212425 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2
    • doi:10.1038/sj.emboj.7601567
    • Stevenson LF, Sparks A, Allende-Vega N, Xirodimas DP, Lane DP, et al. (2007) The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2. EMBO J 26: 976-986. doi:10.1038/sj.emboj.7601567. PubMed: 17290220.
    • (2007) EMBO J , vol.26 , pp. 976-986
    • Stevenson, L.F.1    Sparks, A.2    Allende-Vega, N.3    Xirodimas, D.P.4    Lane, D.P.5
  • 14
    • 83555162507 scopus 로고    scopus 로고
    • Regulation of p53 stability and function by the deubiquitinating enzyme USP42
    • doi:10.1038/emboj.2011.419
    • Hock AK, Vigneron AM, Carter S, Ludwig RL, Vousden KH, (2011) Regulation of p53 stability and function by the deubiquitinating enzyme USP42. EMBO J 30: 4921-4930. doi:10.1038/emboj.2011.419. PubMed: 22085928.
    • (2011) EMBO J , vol.30 , pp. 4921-4930
    • Hock, A.K.1    Vigneron, A.M.2    Carter, S.3    Ludwig, R.L.4    Vousden, K.H.5
  • 15
    • 36448943427 scopus 로고    scopus 로고
    • DUBA: a deubiquitinase that regulates type I interferon production
    • doi:10.1126/science.1145918
    • Kayagaki N, Phung Q, Chan S, Chaudhari R, Quan C, et al. (2007) DUBA: a deubiquitinase that regulates type I interferon production. Science 318: 1628-1632. doi:10.1126/science.1145918. PubMed: 17991829.
    • (2007) Science , vol.318 , pp. 1628-1632
    • Kayagaki, N.1    Phung, Q.2    Chan, S.3    Chaudhari, R.4    Quan, C.5
  • 16
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • doi:10.1016/j.cell.2009.04.042
    • Sowa ME, Bennett EJ, Gygi SP, Harper JW, (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138: 389-403. doi:10.1016/j.cell.2009.04.042. PubMed: 19615732.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 17
    • 76349083381 scopus 로고    scopus 로고
    • ARF antagonizes the ability of Miz-1 to inhibit p53-mediated transactivation
    • doi:10.1038/onc.2009.372
    • Miao L, Song Z, Jin L, Zhu YM, Wen LP, et al. (2010) ARF antagonizes the ability of Miz-1 to inhibit p53-mediated transactivation. Oncogene 29: 711-722. doi:10.1038/onc.2009.372. PubMed: 19901969.
    • (2010) Oncogene , vol.29 , pp. 711-722
    • Miao, L.1    Song, Z.2    Jin, L.3    Zhu, Y.M.4    Wen, L.P.5
  • 18
    • 0021203450 scopus 로고
    • Managing skin damage induced by doxorubicin hydrochloride and daunorubicin hydrochloride
    • Cox RF, (1984) Managing skin damage induced by doxorubicin hydrochloride and daunorubicin hydrochloride. Am J Hosp Pharm. 41(11):: 2410-2414. PubMed: 6150636.
    • (1984) Am J Hosp Pharm , vol.41 , pp. 2410-2414
    • Cox, R.F.1
  • 19
    • 78049302116 scopus 로고    scopus 로고
    • p53 post-translational modification: deregulated in tumorigenesis
    • doi:10.1016/j.molmed.2010.09.002
    • Dai C, Gu W, (2010) p53 post-translational modification: deregulated in tumorigenesis. Trends Mol Med 16: 528-536. doi:10.1016/j.molmed.2010.09.002. PubMed: 20932800.
    • (2010) Trends Mol Med , vol.16 , pp. 528-536
    • Dai, C.1    Gu, W.2
  • 20
    • 0037432773 scopus 로고    scopus 로고
    • Polyubiquitination of p53 by a ubiquitin ligase activity of p300
    • doi:10.1126/science.1080386
    • Grossman SR, Deato ME, Brignone C, Chan HM, Kung AL, et al. (2003) Polyubiquitination of p53 by a ubiquitin ligase activity of p300. Science 300: 342-344. doi:10.1126/science.1080386. PubMed: 12690203.
    • (2003) Science , vol.300 , pp. 342-344
    • Grossman, S.R.1    Deato, M.E.2    Brignone, C.3    Chan, H.M.4    Kung, A.L.5
  • 21
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • doi:10.1038/387296a0
    • Haupt Y, Maya R, Kazaz A, Oren M, (1997) Mdm2 promotes the rapid degradation of p53. Nature 387: 296-299. doi:10.1038/387296a0. PubMed: 9153395.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 22
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • doi:10.1038/387299a0
    • Kubbutat MH, Jones SN, Vousden KH, (1997) Regulation of p53 stability by Mdm2. Nature 387: 299-303. doi:10.1038/387299a0. PubMed: 9153396.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 23
    • 0036849734 scopus 로고    scopus 로고
    • Human papillomavirus immortalization and transformation functions
    • doi:10.1016/S0168-1702(02)00190-9
    • Münger K, Howley PM, (2002) Human papillomavirus immortalization and transformation functions. Virus Res 89: 213-228. doi:10.1016/S0168-1702(02)00190-9. PubMed: 12445661.
    • (2002) Virus Res , vol.89 , pp. 213-228
    • Münger, K.1    Howley, P.M.2
  • 24
    • 70349488818 scopus 로고    scopus 로고
    • CBP and p300 are cytoplasmic E4 polyubiquitin ligases for p53
    • doi:10.1073/pnas.0904305106
    • Shi D, Pop MS, Kulikov R, Love IM, Kung AL, et al. (2009) CBP and p300 are cytoplasmic E4 polyubiquitin ligases for p53. Proc Natl Acad Sci U S A 106: 16275-16280. doi:10.1073/pnas.0904305106. PubMed: 19805293.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 16275-16280
    • Shi, D.1    Pop, M.S.2    Kulikov, R.3    Love, I.M.4    Kung, A.L.5
  • 25
    • 21244451434 scopus 로고    scopus 로고
    • ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
    • doi:10.1016/j.cell.2005.03.037
    • Chen D, Kon N, Li M, Zhang W, Qin J, et al. (2005) ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 121: 1071-1083. doi:10.1016/j.cell.2005.03.037. PubMed: 15989956.
    • (2005) Cell , vol.121 , pp. 1071-1083
    • Chen, D.1    Kon, N.2    Li, M.3    Zhang, W.4    Qin, J.5
  • 26
    • 31544457877 scopus 로고    scopus 로고
    • p53 ubiquitination: Mdm2 and beyond
    • doi:10.1016/j.molcel.2006.01.020
    • Brooks CL, Gu W, (2006) p53 ubiquitination: Mdm2 and beyond. Mol Cell 21: 307-315. doi:10.1016/j.molcel.2006.01.020. PubMed: 16455486.
    • (2006) Mol Cell , vol.21 , pp. 307-315
    • Brooks, C.L.1    Gu, W.2
  • 27
    • 33846193699 scopus 로고    scopus 로고
    • An essential function of the extreme C-terminus of MDM2 can be provided by MDMX
    • doi:10.1038/sj.emboj.7601469
    • Uldrijan S, Pannekoek WJ, Vousden KH, (2007) An essential function of the extreme C-terminus of MDM2 can be provided by MDMX. EMBO J 26: 102-112. doi:10.1038/sj.emboj.7601469. PubMed: 17159902.
    • (2007) EMBO J , vol.26 , pp. 102-112
    • Uldrijan, S.1    Pannekoek, W.J.2    Vousden, K.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.