메뉴 건너뛰기




Volumn 32, Issue 43, 2013, Pages 5167-5175

The deubiquitinating enzyme USP37 regulates the oncogenic fusion protein PLZF/RARA stability

Author keywords

acute promyelocytic leukemia; deubiquitinating enzyme; PLZF; RARA; USP37

Indexed keywords

ARSENIC TRIOXIDE; ONCOPROTEIN; PLZF RARA FUSION PROTEIN; PROTEASOME; PROTEIN USP37; RETINOIC ACID; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84886799764     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2012.537     Document Type: Article
Times cited : (32)

References (32)
  • 1
    • 0037409182 scopus 로고    scopus 로고
    • The molecular pathogenesis of acute promyelocytic leukaemia: Implications for the clinical management of the disease
    • Mistry AR, Pedersen EW, Solomon E, Grimwade D. The molecular pathogenesis of acute promyelocytic leukaemia: Implications for the clinical management of the disease. Blood Rev 2003; 17: 71-97
    • (2003) Blood Rev , vol.17 , pp. 71-97
    • Mistry, A.R.1    Pedersen, E.W.2    Solomon, E.3    Grimwade, D.4
  • 2
    • 0033561797 scopus 로고    scopus 로고
    • Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia
    • Melnick A, Licht JD. Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia. Blood 1999; 93: 3167-3215
    • (1999) Blood , vol.93 , pp. 3167-3215
    • Melnick, A.1    Licht, J.D.2
  • 3
    • 76249123883 scopus 로고    scopus 로고
    • Identification of a myeloid committed progenitor as the cancer-initiating cell in acute promyelocytic leukemia
    • Guibal FC, Alberich-Jorda M, Hirai H, Ebralidze A, Levantini E, Di Ruscio A et al. Identification of a myeloid committed progenitor as the cancer-initiating cell in acute promyelocytic leukemia. Blood 2009; 114: 5415-5425
    • (2009) Blood , vol.114 , pp. 5415-5425
    • Guibal, F.C.1    Alberich-Jorda, M.2    Hirai, H.3    Ebralidze, A.4    Levantini, E.5    Di Ruscio, A.6
  • 4
    • 57349152259 scopus 로고    scopus 로고
    • Eradication of acute promyelocytic leukemia-initiating cells through PML-RARA degradation
    • Nasr R, Guillemin MC, Ferhi O, Soilihi H, Peres L, Berthier C et al. Eradication of acute promyelocytic leukemia-initiating cells through PML-RARA degradation. Nat Med 2008; 14: 1333-1342
    • (2008) Nat Med , vol.14 , pp. 1333-1342
    • Nasr, R.1    Guillemin, M.C.2    Ferhi, O.3    Soilihi, H.4    Peres, L.5    Berthier, C.6
  • 6
    • 41949111045 scopus 로고    scopus 로고
    • Acute promyelocytic leukemia: From highly fatal to highly curable
    • Wang ZY, Chen Z. Acute promyelocytic leukemia: From highly fatal to highly curable. Blood 2008; 111: 2505-2515
    • (2008) Blood , vol.111 , pp. 2505-2515
    • Wang, Z.Y.1    Chen, Z.2
  • 7
    • 43049096803 scopus 로고    scopus 로고
    • Arsenic degrades PML or PML-RARalpha through a SUMO-Triggered RNF4/ubiquitin-mediated pathway
    • Lallemand-Breitenbach V, Jeanne M, Benhenda S, Nasr R, Lei M, Peres L et al. Arsenic degrades PML or PML-RARalpha through a SUMO-Triggered RNF4/ubiquitin-mediated pathway. Nat Cell Biol 2008; 10: 547-555
    • (2008) Nat Cell Biol , vol.10 , pp. 547-555
    • Lallemand-Breitenbach, V.1    Jeanne, M.2    Benhenda, S.3    Nasr, R.4    Lei, M.5    Peres, L.6
  • 8
    • 77950826446 scopus 로고    scopus 로고
    • Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by directly binding PML
    • Zhang XW, Yan XJ, Zhou ZR, Yang FF, Wu ZY, Sun HB et al. Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by directly binding PML. Science 2010; 328: 240-243
    • (2010) Science , vol.328 , pp. 240-243
    • Zhang, X.W.1    Yan, X.J.2    Zhou, Z.R.3    Yang, F.F.4    Wu, Z.Y.5    Sun, H.B.6
  • 9
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction. Physiol Rev 2002; 82: 373-428
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 10
    • 50949126350 scopus 로고    scopus 로고
    • Protein partners of deubiquitinating enzymes
    • Ventii KH, Wilkinson KD. Protein partners of deubiquitinating enzymes. Biochem J 2008; 414: 161-175
    • (2008) Biochem J , vol.414 , pp. 161-175
    • Ventii, K.H.1    Wilkinson, K.D.2
  • 13
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa ME, Bennett EJ, Gygi SP, Harper JW. Defining the human deubiquitinating enzyme interaction landscape. Cell 2009; 138: 389-403
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 14
    • 0035969097 scopus 로고    scopus 로고
    • Transcriptional regulation in acute promyelocytic leukemia
    • Lin RJ, Sternsdorf T, Tini M, Evans RM. Transcriptional regulation in acute promyelocytic leukemia. Oncogene 2001; 20: 7204-7215
    • (2001) Oncogene , vol.20 , pp. 7204-7215
    • Lin, R.J.1    Sternsdorf, T.2    Tini, M.3    Evans, R.M.4
  • 15
    • 0242389807 scopus 로고    scopus 로고
    • C/EBPbeta: A major PML-RARA-responsive gene in retinoic acid-induced differentiation of APL cells
    • Duprez E, Wagner K, Koch H, Tenen DG. C/EBPbeta: A major PML-RARA-responsive gene in retinoic acid-induced differentiation of APL cells. EMBO J 2003; 22: 5806-5816
    • (2003) EMBO J , vol.22 , pp. 5806-5816
    • Duprez, E.1    Wagner, K.2    Koch, H.3    Tenen, D.G.4
  • 16
    • 0030791974 scopus 로고    scopus 로고
    • Immortalization and leukemic transformation of a myelomonocytic precursor by retrovirally transduced HRX-ENL
    • Lavau C, Szilvassy SJ, Slany R, Cleary ML. Immortalization and leukemic transformation of a myelomonocytic precursor by retrovirally transduced HRX-ENL. EMBO J 1997; 16: 4226-4237
    • (1997) EMBO J , vol.16 , pp. 4226-4237
    • Lavau, C.1    Szilvassy, S.J.2    Slany, R.3    Cleary, M.L.4
  • 17
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • Li M, Brooks CL, Kon N, Gu W. A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol Cell 2004; 13: 879-886
    • (2004) Mol Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 18
    • 73849083434 scopus 로고    scopus 로고
    • Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
    • Schwickart M, Huang X, Lill JR, Liu J, Ferrando R, French DM et al. Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 2010; 463: 103-107
    • (2010) Nature , vol.463 , pp. 103-107
    • Schwickart, M.1    Huang, X.2    Lill, J.R.3    Liu, J.4    Ferrando, R.5    French, D.M.6
  • 20
    • 68849126660 scopus 로고    scopus 로고
    • Small-molecule inhibitor of USP7/HAUSP ubiquitin protease stabilizes and activates p53 in cells
    • Colland F, Formstecher E, Jacq X, Reverdy C, Planquette C, Conrath S et al. Small-molecule inhibitor of USP7/HAUSP ubiquitin protease stabilizes and activates p53 in cells. Mol Cancer Ther 2009; 8: 2286-2295
    • (2009) Mol Cancer Ther , vol.8 , pp. 2286-2295
    • Colland, F.1    Formstecher, E.2    Jacq, X.3    Reverdy, C.4    Planquette, C.5    Conrath, S.6
  • 21
    • 77956527159 scopus 로고    scopus 로고
    • Enhancement of proteasome activity by a small-molecule inhibitor of USP14
    • Lee BH, Lee MJ, Park S, Oh DC, Elsasser S, Chen PC et al. Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 2010; 467: 179-184
    • (2010) Nature , vol.467 , pp. 179-184
    • Lee, B.H.1    Lee, M.J.2    Park, S.3    Oh, D.C.4    Elsasser, S.5    Chen, P.C.6
  • 22
    • 79955977893 scopus 로고    scopus 로고
    • Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry
    • Huang X, Summers MK, Pham V, Lill JR, Liu J, Lee G et al. Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry. Mol Cell 2011; 42: 511-523
    • (2011) Mol Cell , vol.42 , pp. 511-523
    • Huang, X.1    Summers, M.K.2    Pham, V.3    Lill, J.R.4    Liu, J.5    Lee, G.6
  • 23
    • 0034548845 scopus 로고    scopus 로고
    • The aberrant fusion proteins PML-RAR alpha and PLZF-RAR alpha contribute to the overexpression of cyclin A1 in acute promyelocytic leukemia
    • Muller C, Yang R, Park DJ, Serve H, Berdel WE, Koeffler HP. The aberrant fusion proteins PML-RAR alpha and PLZF-RAR alpha contribute to the overexpression of cyclin A1 in acute promyelocytic leukemia. Blood 2000; 96: 3894-3899
    • (2000) Blood , vol.96 , pp. 3894-3899
    • Muller, C.1    Yang, R.2    Park, D.J.3    Serve, H.4    Berdel, W.E.5    Koeffler, H.P.6
  • 25
    • 20944448018 scopus 로고    scopus 로고
    • Cyclin A1, the alternative A-Type cyclin, contributes to G1/S cell cycle progression in somatic cells
    • Ji P, Agrawal S, Diederichs S, Baumer N, Becker A, Cauvet T et al. Cyclin A1, the alternative A-Type cyclin, contributes to G1/S cell cycle progression in somatic cells. Oncogene 2005; 24: 2739-2744
    • (2005) Oncogene , vol.24 , pp. 2739-2744
    • Ji, P.1    Agrawal, S.2    Diederichs, S.3    Baumer, N.4    Becker, A.5    Cauvet, T.6
  • 26
    • 69749125286 scopus 로고    scopus 로고
    • PLZF is a regulator of homeostatic and cytokine-induced myeloid development
    • Doulatov S, Notta F, Rice KL, Howell L, Zelent A, Licht JD et al. PLZF is a regulator of homeostatic and cytokine-induced myeloid development. Genes Dev 2009; 23: 2076-2087
    • (2009) Genes Dev , vol.23 , pp. 2076-2087
    • Doulatov, S.1    Notta, F.2    Rice, K.L.3    Howell, L.4    Zelent, A.5    Licht, J.D.6
  • 27
    • 0027411688 scopus 로고
    • Fusion between a novel Kruppel-like zinc finger gene and the retinoic acid receptor-Alpha locus due to a variant t(11;17) translocation associated with acute promyelocytic leukaemia
    • Chen Z, Brand NJ, Chen A, Chen SJ, Tong JH, Wang ZY et al. Fusion between a novel Kruppel-like zinc finger gene and the retinoic acid receptor-Alpha locus due to a variant t(11;17) translocation associated with acute promyelocytic leukaemia. EMBO J 1993; 12: 1161-1167
    • (1993) EMBO J , vol.12 , pp. 1161-1167
    • Chen, Z.1    Brand, N.J.2    Chen, A.3    Chen, S.J.4    Tong, J.H.5    Wang, Z.Y.6
  • 28
    • 0031842974 scopus 로고    scopus 로고
    • The promyelocytic leukemia zinc finger protein affects myeloid cell growth, differentiation, and apoptosis
    • Shaknovich R, Yeyati PL, Ivins S, Melnick A, Lempert C, Waxman S et al. The promyelocytic leukemia zinc finger protein affects myeloid cell growth, differentiation, and apoptosis. Mol Cell Biol 1998; 18: 5533-5545
    • (1998) Mol Cell Biol , vol.18 , pp. 5533-5545
    • Shaknovich, R.1    Yeyati, P.L.2    Ivins, S.3    Melnick, A.4    Lempert, C.5    Waxman, S.6
  • 31
    • 79953331726 scopus 로고    scopus 로고
    • Structural and functional roles of Daxx SIM phosphorylation in SUMO paralog-selective binding and apoptosis modulation
    • Chang CC, Naik MT, Huang YS, Jeng JC, Liao PH, Kuo HY et al. Structural and functional roles of Daxx SIM phosphorylation in SUMO paralog-selective binding and apoptosis modulation. Mol Cell 2011; 42: 62-74
    • (2011) Mol Cell , vol.42 , pp. 62-74
    • Chang, C.C.1    Naik, M.T.2    Huang, Y.S.3    Jeng, J.C.4    Liao, P.H.5    Kuo, H.Y.6
  • 32
    • 33750491062 scopus 로고    scopus 로고
    • Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors
    • Lin DY, Huang YS, Jeng JC, Kuo HY, Chang CC, Chao TT et al. Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol Cell 2006; 24: 341-354
    • (2006) Mol Cell , vol.24 , pp. 341-354
    • Lin, D.Y.1    Huang, Y.S.2    Jeng, J.C.3    Kuo, H.Y.4    Chang, C.C.5    Chao, T.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.