메뉴 건너뛰기




Volumn 8, Issue 8, 2009, Pages 2286-2295

Small-molecule inhibitor of USP7/HAUSP ubiquitin protease stabilizes and activates p53 in cells

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 10A; CALPAIN 1; CASPASE 3; CATHEPSIN B; CATHEPSIN D; CATHEPSIN E; CATHEPSIN L; CATHEPSIN S; DIPEPTIDYL CARBOXYPEPTIDASE; HBX 41108; PHOSPHATIDYLINOSITOL 3 KINASE; PLASMIN; PROTEASOME; PROTEIN KINASE B; PROTEIN MDM2; PROTEIN P53; PROTEINASE; PROTEINASE INHIBITOR; RENIN; THROMBIN; TRYPSIN; UBIQUITIN; UBIQUITIN SPECIFIC PROTEASE 7; UNCLASSIFIED DRUG;

EID: 68849126660     PISSN: 15357163     EISSN: None     Source Type: Journal    
DOI: 10.1158/1535-7163.MCT-09-0097     Document Type: Article
Times cited : (270)

References (35)
  • 1
    • 33748991453 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins in cancer pathogenesis
    • Hoeller D, Hecker CM, Dikic I. Ubiquitin and ubiquitin-like proteins in cancer pathogenesis. Nat Rev Cancer 2006;6:776-88.
    • (2006) Nat Rev Cancer , vol.6 , pp. 776-788
    • Hoeller, D.1    Hecker, C.M.2    Dikic, I.3
  • 2
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein DC. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006;443:780-6.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 3
    • 33645823654 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in viral infections
    • Gao G, Luo H. The ubiquitin-proteasome pathway in viral infections. Can J Physiol Pharmacol 2006;84:5-14.
    • (2006) Can J Physiol Pharmacol , vol.84 , pp. 5-14
    • Gao, G.1    Luo, H.2
  • 4
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: A suitable antineoplastic target
    • Adams J. The proteasome: a suitable antineoplastic target. Nat Rev Cancer 2004;4:349-60.
    • (2004) Nat Rev Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 5
    • 0033152760 scopus 로고    scopus 로고
    • Proteasome inhibitors: A novel class of potent and effective antitumor agents
    • Adams J, Palombella VJ, Sausville EA, et al. Proteasome inhibitors: a novel class of potent and effective antitumor agents. Cancer Res 1999;59:2615-22.
    • (1999) Cancer Res , vol.59 , pp. 2615-2622
    • Adams, J.1    Palombella, V.J.2    Sausville, E.A.3
  • 6
    • 28344456279 scopus 로고    scopus 로고
    • A genomic and functional inventory of deubiquitinating enzymes
    • Nijman SM, Luna-Vargas MP, Velds A, et al. A genomic and functional inventory of deubiquitinating enzymes. Cell 2005;123:773-86.
    • (2005) Cell , vol.123 , pp. 773-786
    • Nijman, S.M.1    Luna-Vargas, M.P.2    Velds, A.3
  • 7
    • 38849110179 scopus 로고    scopus 로고
    • Targeting ubiquitin specific proteases for drug discovery
    • Daviet L, Colland F. Targeting ubiquitin specific proteases for drug discovery. Biochimie 2008;90:270-83.
    • (2008) Biochimie , vol.90 , pp. 270-283
    • Daviet, L.1    Colland, F.2
  • 8
    • 0031023690 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein
    • Everett RD, Meredith M, Orr A, Cross A, Kathoria M, Parkinson J. A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J 1997;16:1519-30.
    • (1997) EMBO J , vol.16 , pp. 1519-1530
    • Everett, R.D.1    Meredith, M.2    Orr, A.3    Cross, A.4    Kathoria, M.5    Parkinson, J.6
  • 9
    • 0041529593 scopus 로고    scopus 로고
    • Protein profiling with Epstein-Barr nuclear antigen-1 reveals an interaction with the herpesvirus-associated ubiquitin-specific protease HAUSP/USP7
    • Holowaty MN, Zeghouf M, Wu H, et al. Protein profiling with Epstein-Barr nuclear antigen-1 reveals an interaction with the herpesvirus-associated ubiquitin-specific protease HAUSP/USP7. J Biol Chem 2003;278:29987-94.
    • (2003) J Biol Chem , vol.278 , pp. 29987-29994
    • Holowaty, M.N.1    Zeghouf, M.2    Wu, H.3
  • 11
    • 3242774545 scopus 로고    scopus 로고
    • HAUSP is required for p53 destabilization
    • Cummins JM, Vogelstein B. HAUSP is required for p53 destabilization. Cell Cycle 2004;3:689-92.
    • (2004) Cell Cycle , vol.3 , pp. 689-692
    • Cummins, J.M.1    Vogelstein, B.2
  • 12
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-2 pathway
    • Li M, Brooks CL, Kon N, Gu W. A dynamic role of HAUSP in the p53-2 pathway. Mol Cell 2004;13:879-86.
    • (2004) Mol Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 13
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li M, Chen D, Shiloh A, et al. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 2002;416:648-53.
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3
  • 14
    • 33244490784 scopus 로고    scopus 로고
    • Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: Implications for the regulation of the p53-MDM2 pathway
    • Hu M, Gu L, Li M, Jeffrey PD, Gu W, Shi Y. Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway. PLoS Biol 2006;4:e27.
    • (2006) PLoS Biol , vol.4
    • Hu, M.1    Gu, L.2    Li, M.3    Jeffrey, P.D.4    Gu, W.5    Shi, Y.6
  • 15
    • 33644951846 scopus 로고    scopus 로고
    • Colland F. Ubiquitin and cancer: from molecular targets and mechanisms to the clinic - AACR Special Conference. IDrugs 2006;9:179-81.
    • Colland F. Ubiquitin and cancer: from molecular targets and mechanisms to the clinic - AACR Special Conference. IDrugs 2006;9:179-81.
  • 16
    • 44349179787 scopus 로고    scopus 로고
    • A role of HAUSP in tumor suppression in a human colon carcinoma xenograft model
    • Becker K, Marchenko ND, Palacios G, Moll UM. A role of HAUSP in tumor suppression in a human colon carcinoma xenograft model. Cell Cycle 2008;7:1205-13.
    • (2008) Cell Cycle , vol.7 , pp. 1205-1213
    • Becker, K.1    Marchenko, N.D.2    Palacios, G.3    Moll, U.M.4
  • 17
    • 33749188883 scopus 로고    scopus 로고
    • FOXO4 transcriptional activity is regulated by monoubiquitination and USP7/HAUSP
    • van der Horst A, de Vries-Smits AM, Brenkman AB, et al. FOXO4 transcriptional activity is regulated by monoubiquitination and USP7/HAUSP. Nat Cell Biol 2006;8:1064-73.
    • (2006) Nat Cell Biol , vol.8 , pp. 1064-1073
    • van der Horst, A.1    de Vries-Smits, A.M.2    Brenkman, A.B.3
  • 18
    • 53649106156 scopus 로고    scopus 로고
    • The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network
    • Song MS, Salmena L, Carracedo A, et al. The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network. Nature 2008;455:813-7.
    • (2008) Nature , vol.455 , pp. 813-817
    • Song, M.S.1    Salmena, L.2    Carracedo, A.3
  • 19
    • 33847276654 scopus 로고    scopus 로고
    • Monoubiquitylation promotes mitochondrial p53 translocation
    • Marchenko ND, Wolff S, Erster S, Becker K, Moll UM. Monoubiquitylation promotes mitochondrial p53 translocation. EMBO J 2007;26:923-34.
    • (2007) EMBO J , vol.26 , pp. 923-934
    • Marchenko, N.D.1    Wolff, S.2    Erster, S.3    Becker, K.4    Moll, U.M.5
  • 20
    • 19444367393 scopus 로고    scopus 로고
    • Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2
    • Meulmeester E, Maurice MM, Boutell C, et al. Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2. Mol Cell 2005;18:565-76.
    • (2005) Mol Cell , vol.18 , pp. 565-576
    • Meulmeester, E.1    Maurice, M.M.2    Boutell, C.3
  • 21
    • 0032539582 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes
    • Dang LC, Melandri FD, Stein RL. Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes. Biochemistry 1998;37:1868-79.
    • (1998) Biochemistry , vol.37 , pp. 1868-1879
    • Dang, L.C.1    Melandri, F.D.2    Stein, R.L.3
  • 22
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang JH, Chung TD, Oldenburg KR. A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J Biomol Screen 1999;4:67-73.
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 23
    • 33749628876 scopus 로고    scopus 로고
    • Managing, profiling and analyzing a library of 2.6 million compounds gathered from 32 chemical providers
    • Monge A, Arrault A, Marot C, Morin-Allory L. Managing, profiling and analyzing a library of 2.6 million compounds gathered from 32 chemical providers. Mol Divers 2006;10:389-403.
    • (2006) Mol Divers , vol.10 , pp. 389-403
    • Monge, A.1    Arrault, A.2    Marot, C.3    Morin-Allory, L.4
  • 24
    • 12444269118 scopus 로고    scopus 로고
    • Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line
    • Liu Y, Lashuel HA, Choi S, et al. Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line. Chem Biol 2003;10:837-46.
    • (2003) Chem Biol , vol.10 , pp. 837-846
    • Liu, Y.1    Lashuel, H.A.2    Choi, S.3
  • 25
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu M, Li P, Li M, et al. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 2002;111:1041-54.
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3
  • 27
    • 0037763817 scopus 로고    scopus 로고
    • Comparative evaluation of 11 scoring functions for molecular docking
    • Wang R, Lu Y, Wang S. Comparative evaluation of 11 scoring functions for molecular docking. J Med Chem 2003;46:2287-303.
    • (2003) J Med Chem , vol.46 , pp. 2287-2303
    • Wang, R.1    Lu, Y.2    Wang, S.3
  • 28
    • 0242361216 scopus 로고    scopus 로고
    • Semi-synthesis, topoisomerase I and kinases inhibitory properties, and antiproliferative activities of new rebeccamycin derivatives
    • Moreau P, Gaillard N, Marminon C, et al. Semi-synthesis, topoisomerase I and kinases inhibitory properties, and antiproliferative activities of new rebeccamycin derivatives. Bioorg Med Chem 2003;11:4871-9.
    • (2003) Bioorg Med Chem , vol.11 , pp. 4871-4879
    • Moreau, P.1    Gaillard, N.2    Marminon, C.3
  • 29
    • 0032701521 scopus 로고    scopus 로고
    • Disruption of p53 in human cancer cells alters the responses to therapeutic agents
    • Bunz F, Hwang PM, Torrance C, et al. Disruption of p53 in human cancer cells alters the responses to therapeutic agents. J Clin Invest 1999;104:263-9.
    • (1999) J Clin Invest , vol.104 , pp. 263-269
    • Bunz, F.1    Hwang, P.M.2    Torrance, C.3
  • 30
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B, et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 2004;303:844-8.
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 31
    • 33646550549 scopus 로고    scopus 로고
    • MDM2 antagonists activate p53 and synergize with genotoxic drugs in B-cell chronic lymphocytic leukemia cells
    • Coll-Mulet L, Iglesias-Serret D, Santidrian AF, et al. MDM2 antagonists activate p53 and synergize with genotoxic drugs in B-cell chronic lymphocytic leukemia cells. Blood 2006;107:4109-14.
    • (2006) Blood , vol.107 , pp. 4109-4114
    • Coll-Mulet, L.1    Iglesias-Serret, D.2    Santidrian, A.F.3
  • 32
    • 20444369867 scopus 로고    scopus 로고
    • Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells
    • Yang Y, Ludwig RL, Jensen JP, et al. Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells. Cancer Cell 2005;7:547-59.
    • (2005) Cancer Cell , vol.7 , pp. 547-559
    • Yang, Y.1    Ludwig, R.L.2    Jensen, J.P.3
  • 33
    • 33845611951 scopus 로고    scopus 로고
    • Modeling the therapeutic efficacy of p53 restoration in tumors
    • Martins CP, Brown-Swigart L, Evan GI. Modeling the therapeutic efficacy of p53 restoration in tumors. Cell 2006;127:1323-34.
    • (2006) Cell , vol.127 , pp. 1323-1334
    • Martins, C.P.1    Brown-Swigart, L.2    Evan, G.I.3
  • 34
    • 33845185824 scopus 로고    scopus 로고
    • Mdm2 is critically and continuously required to suppress lethal p53 activity in vivo
    • Ringshausen I, O'Shea CC, Finch AJ, Swigart LB, Evan GI. Mdm2 is critically and continuously required to suppress lethal p53 activity in vivo. Cancer Cell 2006;10:501-14.
    • (2006) Cancer Cell , vol.10 , pp. 501-514
    • Ringshausen, I.1    O'Shea, C.C.2    Finch, A.J.3    Swigart, L.B.4    Evan, G.I.5
  • 35
    • 14644406268 scopus 로고    scopus 로고
    • GMP synthetase stimulates histone H2B deubiquitylation by the epigenetic silencer USP7
    • van der Knaap JA, Kumar BR, Moshkin YM, et al. GMP synthetase stimulates histone H2B deubiquitylation by the epigenetic silencer USP7. Mol Cell 2005;17:695-707.
    • (2005) Mol Cell , vol.17 , pp. 695-707
    • van der Knaap, J.A.1    Kumar, B.R.2    Moshkin, Y.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.