메뉴 건너뛰기




Volumn 23, Issue 5, 2013, Pages 620-634

Def defines a conserved nucleolar pathway that leads p53 to proteasome-independent degradation

Author keywords

133p53 113p53; Calpain; Def; digestive organ development; nucleolus; p53; ubquitination

Indexed keywords

DANIO RERIO;

EID: 84877144820     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2013.16     Document Type: Article
Times cited : (56)

References (36)
  • 1
    • 33646807832 scopus 로고    scopus 로고
    • The P53 pathway: What questions remain to be explored?
    • Levine AJ, Hu W, Feng Z. The P53 pathway: what questions remain to be explored? Cell Death Differ 2006; 13:1027-1036.
    • (2006) Cell Death Differ , vol.13 , pp. 1027-1036
    • Levine, A.J.1    Hu, W.2    Feng, Z.3
  • 2
    • 67650886073 scopus 로고    scopus 로고
    • TRIMming p53 for ubiquitination
    • Tai E, Benchimol S. TRIMming p53 for ubiquitination. Proc Natl Acad Sci USA 2009; 106:11431-11432.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11431-11432
    • Tai, E.1    Benchimol, S.2
  • 3
    • 77449127476 scopus 로고    scopus 로고
    • Ubiquitin-independent p53 proteasomal degradation
    • Tsvetkov P, Reuven N, Shaul Y. Ubiquitin-independent p53 proteasomal degradation. Cell Death Differ 2010; 17:103-108.
    • (2010) Cell Death Differ , vol.17 , pp. 103-108
    • Tsvetkov, P.1    Reuven, N.2    Shaul, Y.3
  • 4
    • 0030987086 scopus 로고    scopus 로고
    • Proteolysis by calpains: A possible contribution to degradation of p53
    • Pariat M, Carillo S, Molinari M, et al. Proteolysis by calpains: a possible contribution to degradation of p53. Mol Cell Biol 1997; 17:2806-2815.
    • (1997) Mol Cell Biol , vol.17 , pp. 2806-2815
    • Pariat, M.1    Carillo, S.2    Molinari, M.3
  • 5
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat MH, Vousden KH. Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol Cell Biol 1997; 17:460-468.
    • (1997) Mol Cell Biol , vol.17 , pp. 460-468
    • Kubbutat, M.H.1    Vousden, K.H.2
  • 6
    • 0030992491 scopus 로고    scopus 로고
    • On the involvement of calpains in the degradation of the tumor suppressor protein p53
    • Gonen H, Shkedy D, Barnoy S, Kosower NS, Ciechanover A. On the involvement of calpains in the degradation of the tumor suppressor protein p53. FEBS Lett 1997; 406:17-22.
    • (1997) FEBS Lett , vol.406 , pp. 17-22
    • Gonen, H.1    Shkedy, D.2    Barnoy, S.3    Kosower, N.S.4    Ciechanover, A.5
  • 7
    • 77956365523 scopus 로고    scopus 로고
    • Role of calpain-mediated p53 truncation in semaphorin 3A-induced axonal growth regulation
    • Qin Q, Liao G, Baudry M and Bi X. Role of calpain-mediated p53 truncation in semaphorin 3A-induced axonal growth regulation. Proc Natl Acad Sci USA 2012; 107:13883-13887.
    • (2012) Proc Natl Acad Sci USA , vol.107 , pp. 13883-13887
    • Qin, Q.1    Liao, G.2    Baudry, M.3    Bi, X.4
  • 10
    • 7244238177 scopus 로고    scopus 로고
    • Inhibition of MDM2-mediated p53 ubiquitina-tion and degradation by ribosomal protein L5
    • Dai MS, Lu H. Inhibition of MDM2-mediated p53 ubiquitina-tion and degradation by ribosomal protein L5. J Biol Chem 2004; 279:44475-44482.
    • (2004) J Biol Chem , vol.279 , pp. 44475-44482
    • Dai, M.S.1    Lu, H.2
  • 11
    • 0038724615 scopus 로고    scopus 로고
    • Regulation of HDM2 activity by the ribosomal protein L11
    • Lohrum MAE, Ludwig RL, Kubbutat MHG, Hanlon M, Vous-den KH. Regulation of HDM2 activity by the ribosomal protein L11. Cancer Cell 2003; 3:577-587.
    • (2003) Cancer Cell , vol.3 , pp. 577-587
    • Mae, L.1    Ludwig, R.L.2    Mhg, K.3    Hanlon, M.4    Vous-Den, K.H.5
  • 12
    • 84861170072 scopus 로고    scopus 로고
    • Suprainduc-tion of p53 by disruption of 40S and 60S ribosome biogenesis leads to the activation of a novel G2/M checkpoint
    • Fumagalli S, Ivanenkov VV, Teng T, Thomas G. Suprainduc-tion of p53 by disruption of 40S and 60S ribosome biogenesis leads to the activation of a novel G2/M checkpoint. Genes Dev 2012; 26:1028-1040.
    • (2012) Genes Dev , vol.26 , pp. 1028-1040
    • Fumagalli, S.1    Ivanenkov, V.V.2    Teng, T.3    Thomas, G.4
  • 13
    • 28444434535 scopus 로고    scopus 로고
    • Loss of function of def selectively up-regulates Delta113p53 expression to arrest expansion growth of digestive organs in zebrafsh
    • Chen J, Ruan H, Ng SM, et al. Loss of function of def selectively up-regulates Delta113p53 expression to arrest expansion growth of digestive organs in zebrafsh. Genes Dev 2005; 19:2900-2911.
    • (2005) Genes Dev , vol.19 , pp. 2900-2911
    • Chen, J.1    Ruan, H.2    Ng, S.M.3
  • 14
    • 78149312601 scopus 로고    scopus 로고
    • The DEAD-box RNA helicase-like Utp25 is an SSU processome component
    • Charette JM, Baserga SJ. The DEAD-box RNA helicase-like Utp25 is an SSU processome component. RNA 2010; 16:2156-2169.
    • (2010) RNA , vol.16 , pp. 2156-2169
    • Charette, J.M.1    Baserga, S.J.2
  • 15
    • 77953570299 scopus 로고    scopus 로고
    • Utp25p, a nucleolar Saccharo-myces cerevisiae protein, interacts with U3 snoRNP subunits and affects processing of the 35S pre-rRNA
    • Goldfeder MB, Oliveira CC. Utp25p, a nucleolar Saccharo-myces cerevisiae protein, interacts with U3 snoRNP subunits and affects processing of the 35S pre-rRNA. FEBS J 2010; 277:2838-2852.
    • (2010) FEBS J , vol.277 , pp. 2838-2852
    • Goldfeder, M.B.1    Oliveira, C.C.2
  • 16
    • 77958477288 scopus 로고    scopus 로고
    • NOF1 encodes an Arabidopsis protein involved in the control of rRNA expression
    • Harscoet E, Dubreucq B, Palauqui JC, Lepiniec L. NOF1 encodes an Arabidopsis protein involved in the control of rRNA expression. PLoS One 2010; 5:e12829.
    • (2010) PLoS One , vol.5
    • Harscoet, E.1    Dubreucq, B.2    Palauqui, J.C.3    Lepiniec, L.4
  • 17
    • 59949088362 scopus 로고    scopus 로고
    • P53 isoform delta113p53 is a p53 target gene that antagonizes p53 apoptotic activity via BclxL activation in zebrafsh
    • Chen J, Ng SM, Chang C, et al. p53 isoform delta113p53 is a p53 target gene that antagonizes p53 apoptotic activity via BclxL activation in zebrafsh. Genes Dev 2009; 23:278-290.
    • (2009) Genes Dev , vol.23 , pp. 278-290
    • Chen, J.1    Ng, S.M.2    Chang, C.3
  • 18
    • 24344448786 scopus 로고    scopus 로고
    • P53 isoforms can regulate p53 transcriptional activity
    • Bourdon JC, Fernandes K, Murray-Zmijewski F, et al. p53 isoforms can regulate p53 transcriptional activity. Genes Dev 2005; 19:2122-2137.
    • (2005) Genes Dev , vol.19 , pp. 2122-2137
    • Bourdon, J.C.1    Fernandes, K.2    Murray-Zmijewski, F.3
  • 19
    • 78651277059 scopus 로고    scopus 로고
    • P53 directly transactivates Delta133p53alpha, regulating cell fate outcome in response to DNA damage
    • Aoubala M, Murray-Zmijewski F, Khoury MP, et al. p53 directly transactivates Delta133p53alpha, regulating cell fate outcome in response to DNA damage. Cell Death Differ 2011; 18:248-258.
    • (2011) Cell Death Differ , vol.18 , pp. 248-258
    • Aoubala, M.1    Murray-Zmijewski, F.2    Khoury, M.P.3
  • 20
  • 24
    • 0034595214 scopus 로고    scopus 로고
    • Rcl1p, the yeast protein similar to the RNA 3′-phosphate cyclase, associates with U3 snoRNP and is required for 18S rRNA biogenesis
    • Billy E, Wegierski T, Nasr F, Filipowicz W. Rcl1p, the yeast protein similar to the RNA 3′-phosphate cyclase, associates with U3 snoRNP and is required for 18S rRNA biogenesis. EMBO J 2000; 19:2115-2126.
    • (2000) EMBO J , vol.19 , pp. 2115-2126
    • Billy, E.1    Wegierski, T.2    Nasr, F.3    Filipowicz, W.4
  • 25
    • 19944426854 scopus 로고    scopus 로고
    • Tp53 mutant zebrafsh develop malignant peripheral nerve sheath tumors
    • Berghmans S, Murphey RD, Wienholds E, et al. tp53 mutant zebrafsh develop malignant peripheral nerve sheath tumors. Proc Natl Acad Sci USA 2005; 102:407-412.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 407-412
    • Berghmans, S.1    Murphey, R.D.2    Wienholds, E.3
  • 26
    • 78049302116 scopus 로고    scopus 로고
    • P53 post-translational modifcation: Deregulated in tumorigenesis
    • Dai C, Gu W. p53 post-translational modifcation: deregulated in tumorigenesis. Trends Mol Med 2010; 16:528-536.
    • (2010) Trends Mol Med , vol.16 , pp. 528-536
    • Dai, C.1    Gu, W.2
  • 27
    • 0036898541 scopus 로고    scopus 로고
    • Zebrafish as a model organism for the identification and characterization of drugs and genes affecting p53 signaling
    • Langheinrich U, Hennen E, Stott G, Vacun G. Zebrafish as a model organism for the identification and characterization of drugs and genes affecting p53 signaling. Curr Biol 2002;12:2023-2028.
    • (2002) Curr Biol , vol.12 , pp. 2023-2028
    • Langheinrich, U.1    Hennen, E.2    Stott, G.3    Vacun, G.4
  • 28
    • 0036128899 scopus 로고    scopus 로고
    • Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound
    • Bykov VJ, Issaeva N, Shilov A, et al. Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound. Nat Med 2002; 8:282-288.
    • (2002) Nat Med , vol.8 , pp. 282-288
    • Bykov, V.J.1    Issaeva, N.2    Shilov, A.3
  • 29
    • 77749343029 scopus 로고    scopus 로고
    • Analysis of the DNA-binding activity of p53 mutants using functional protein microarrays and its relationship to transcriptional activation
    • Malcikova J, Tichy B, Damborsky J, et al. Analysis of the DNA-binding activity of p53 mutants using functional protein microarrays and its relationship to transcriptional activation. Biol Chem 2010; 391:197-205.
    • (2010) Biol Chem , vol.391 , pp. 197-205
    • Malcikova, J.1    Tichy, B.2    Damborsky, J.3
  • 30
    • 79960104591 scopus 로고    scopus 로고
    • Impact of genetic insights into calpain biology
    • Sorimachi H, Hata S, Ono Y. Impact of genetic insights into calpain biology. J Biochem 2011; 150:23-37.
    • (2011) J Biochem , vol.150 , pp. 23-37
    • Sorimachi, H.1    Hata, S.2    Ono, Y.3
  • 31
    • 66749173427 scopus 로고    scopus 로고
    • Novel variants of muscle calpain 3 identifed in human melanoma cells: Cisplatin-induced changes in vitro and differential expression in melanocytic lesions
    • Moretti D, Del BB, Cosci E, Biagioli M, Miracco C, Mael-laro E. Novel variants of muscle calpain 3 identifed in human melanoma cells: cisplatin-induced changes in vitro and differential expression in melanocytic lesions. Carcinogenesis 2009; 30:960-967.
    • (2009) Carcinogenesis , vol.30 , pp. 960-967
    • Moretti, D.1    Del, B.B.2    Cosci, E.3    Biagioli, M.4    Miracco, C.5    Mael-Laro, E.6
  • 32
    • 0027276561 scopus 로고
    • Muscle-specifc calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle
    • Sorimachi H, Toyama-Sorimachi N, Saido TC, et al. Muscle-specifc calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle. J Biol Chem 1993; 268:10593-10605.
    • (1993) J Biol Chem , vol.268 , pp. 10593-10605
    • Sorimachi, H.1    Toyama-Sorimachi, N.2    Saido, T.C.3
  • 33
    • 3242725958 scopus 로고    scopus 로고
    • Null mutation of calpain 3 (p94) in mice causes abnormal sarco-mere formation in vivo and in vitro
    • Kramerova I, Kudryashova E, Tidball JG, Spencer MJ. Null mutation of calpain 3 (p94) in mice causes abnormal sarco-mere formation in vivo and in vitro. Hum Mol Genet 2004; 13:1373-1388.
    • (2004) Hum Mol Genet , vol.13 , pp. 1373-1388
    • Kramerova, I.1    Kudryashova, E.2    Tidball, J.G.3    Spencer, M.J.4
  • 34
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M, Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 2007; 24:1596-1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 35
    • 67449128692 scopus 로고    scopus 로고
    • Wnt5A activates the calpain-mediated cleavage of flamin A
    • O'Connell MP, Fiori JL, Baugher KM, et al. Wnt5A activates the calpain-mediated cleavage of flamin A. J Invest Dermatol 2009; 129:1782-1789.
    • (2009) J Invest Dermatol , vol.129 , pp. 1782-1789
    • O'Connell, M.P.1    Fiori, J.L.2    Baugher, K.M.3
  • 36
    • 78449292592 scopus 로고    scopus 로고
    • Calpain 2 is required for glio-blastoma cell invasion: Regulation of matrix metalloproteinase 2
    • Jang HS, Lal S, Greenwood JA. Calpain 2 is required for glio-blastoma cell invasion: regulation of matrix metalloproteinase 2. Neurochem Res 2010; 35:1796-1804.
    • (2010) Neurochem Res , vol.35 , pp. 1796-1804
    • Jang, H.S.1    Lal, S.2    Greenwood, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.