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Volumn 402, Issue 5, 2010, Pages 825-837

Further Insight into Substrate Recognition by USP7: Structural and Biochemical Analysis of the HdmX and Hdm2 Interactions with USP7

Author keywords

Hdm2; HdmX; Protein protein interactions; Structural biology; USP7 HAUSP

Indexed keywords

EPSTEIN BARR VIRUS ANTIGEN 1; PROTEIN HDMX; PROTEIN MDM2; PROTEIN P53; PROTEIN USP7; PROTEINASE; SERINE; UNCLASSIFIED DRUG; MDM2 PROTEIN, HUMAN; MDM4 PROTEIN, HUMAN; NUCLEAR PROTEIN; ONCOPROTEIN; PROTEIN BINDING; UBIQUITIN THIOLESTERASE; USP7 PROTEIN, HUMAN;

EID: 77957220495     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.08.017     Document Type: Article
Times cited : (42)

References (33)
  • 1
    • 0028268666 scopus 로고
    • Herpes simplex virus type 1 immediate-early protein Vmw110 binds strongly and specifically to a 135-kDa cellular protein
    • Meredith M., Orr A., Everett R. Herpes simplex virus type 1 immediate-early protein Vmw110 binds strongly and specifically to a 135-kDa cellular protein. Virology 1994, 200:457-469.
    • (1994) Virology , vol.200 , pp. 457-469
    • Meredith, M.1    Orr, A.2    Everett, R.3
  • 2
    • 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 M.N., Zeghouf M., Wu H., Tellam J., Athanasopoulos V., Greenblatt J., Frappier L. Protein profiling with Epstein-Barr nuclear antigen-1 reveals an interaction with the herpesvirus-associated ubiquitin-specific protease HAUSP/USP7. J. Biol. Chem. 2003, 278:29987-29994.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29987-29994
    • Holowaty, M.N.1    Zeghouf, M.2    Wu, H.3    Tellam, J.4    Athanasopoulos, V.5    Greenblatt, J.6    Frappier, L.7
  • 3
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li M., Chen D., Shiloh A., Luo J., Nikolaev A.Y., Qin J., Gu W. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 2002, 416:648-653.
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 5
    • 19444367393 scopus 로고    scopus 로고
    • Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2
    • Meulmeester E., Maurice M.M., Boutell C., Teu-nisse A.F., Ovaa H., Abraham T.E., et al. Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2. Mol. Cell 2005, 18:565-576.
    • (2005) Mol. Cell , vol.18 , pp. 565-576
    • Meulmeester, E.1    Maurice, M.M.2    Boutell, C.3    Teu-nisse, A.F.4    Ovaa, H.5    Abraham, T.E.6
  • 7
    • 0037459377 scopus 로고    scopus 로고
    • Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation
    • Leng R.P., Lin Y., Ma W., Wu H., Lemmers B., Chung S., et al. Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. Cell 2003, 112:779-791.
    • (2003) Cell , vol.112 , pp. 779-791
    • Leng, R.P.1    Lin, Y.2    Ma, W.3    Wu, H.4    Lemmers, B.5    Chung, S.6
  • 8
    • 5644302246 scopus 로고    scopus 로고
    • COP1, the negative regulator of p53, is overexpressed in breast and ovarian adenocarcinomas
    • Dornan D., Bheddah S., Newton K., Ince W., Frantz G.D., Dowd P., et al. COP1, the negative regulator of p53, is overexpressed in breast and ovarian adenocarcinomas. Cancer Res. 2004, 64:7226-7230.
    • (2004) Cancer Res. , vol.64 , pp. 7226-7230
    • Dornan, D.1    Bheddah, S.2    Newton, K.3    Ince, W.4    Frantz, G.D.5    Dowd, P.6
  • 9
    • 0033963335 scopus 로고    scopus 로고
    • MdmX protects p53 from Mdm2-mediated degradation
    • Jackson M.W., Berberich S.J. MdmX protects p53 from Mdm2-mediated degradation. Mol. Cell. Biol. 2000, 20:1001-1007.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1001-1007
    • Jackson, M.W.1    Berberich, S.J.2
  • 11
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones S.N., Roe A.E., Donehower L.A., Bradley A. Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 1995, 378:206-208.
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 12
    • 0034863683 scopus 로고    scopus 로고
    • Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53
    • Parant J., Chavez-Reyes A., Little N.A., Yan W., Reinke V., Jochemsen A.G., Lozano G. Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53. Nat. Genet. 2001, 29:92-95.
    • (2001) Nat. Genet. , vol.29 , pp. 92-95
    • Parant, J.1    Chavez-Reyes, A.2    Little, N.A.3    Yan, W.4    Reinke, V.5    Jochemsen, A.G.6    Lozano, G.7
  • 13
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997, 387:296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 14
    • 0042592947 scopus 로고    scopus 로고
    • MDM2 promotes ubiquitination and degradation of MDMX
    • Pan Y., Chen J. MDM2 promotes ubiquitination and degradation of MDMX. Mol. Cell. Biol. 2003, 23:5113-5121.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5113-5121
    • Pan, Y.1    Chen, J.2
  • 15
    • 0030860911 scopus 로고    scopus 로고
    • Repression of p53-mediated transcription by MDM2: a dual mechanism
    • Thut C.J., Goodrich J.A., Tjian R. Repression of p53-mediated transcription by MDM2: a dual mechanism. Genes Dev. 1997, 11:1974-1986.
    • (1997) Genes Dev. , vol.11 , pp. 1974-1986
    • Thut, C.J.1    Goodrich, J.A.2    Tjian, R.3
  • 16
    • 0035339357 scopus 로고    scopus 로고
    • ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage
    • Maya R., Balass M., Kim S.T., Shkedy D., Leal J.F., Shifman O., et al. ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage. Genes Dev. 2001, 15:1067-1077.
    • (2001) Genes Dev. , vol.15 , pp. 1067-1077
    • Maya, R.1    Balass, M.2    Kim, S.T.3    Shkedy, D.4    Leal, J.F.5    Shifman, O.6
  • 18
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • Li M., Brooks C.L., 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
  • 19
    • 20144386721 scopus 로고    scopus 로고
    • Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization
    • Saridakis V., Sheng Y., Sarkari F., Holowaty M.N., Shire K., Nguyen T., et al. Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization. Mol. Cell 2005, 18:25-36.
    • (2005) Mol. Cell , vol.18 , pp. 25-36
    • Saridakis, V.1    Sheng, Y.2    Sarkari, F.3    Holowaty, M.N.4    Shire, K.5    Nguyen, T.6
  • 21
    • 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 P.D., 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
  • 22
    • 27144444111 scopus 로고    scopus 로고
    • ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage
    • Chen L., Gilkes D.M., Pan Y., Lane W.S., Chen J. ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage. EMBO J. 2005, 24:3411-3422.
    • (2005) EMBO J. , vol.24 , pp. 3411-3422
    • Chen, L.1    Gilkes, D.M.2    Pan, Y.3    Lane, W.S.4    Chen, J.5
  • 23
    • 0001033803 scopus 로고    scopus 로고
    • Structural basis for self-association and receptor recognition of human TRAF2
    • Park Y.C., Burkitt V., Villa A.R., Tong L., Wu H. Structural basis for self-association and receptor recognition of human TRAF2. Nature 1999, 398:533-538.
    • (1999) Nature , vol.398 , pp. 533-538
    • Park, Y.C.1    Burkitt, V.2    Villa, A.R.3    Tong, L.4    Wu, H.5
  • 24
    • 0033197872 scopus 로고    scopus 로고
    • The structural basis for the recognition of diverse receptor sequences by TRAF2
    • Ye H., Park Y.C., Kreishman M., Kieff E., Wu H. The structural basis for the recognition of diverse receptor sequences by TRAF2. Mol. Cell 1999, 4:321-330.
    • (1999) Mol. Cell , vol.4 , pp. 321-330
    • Ye, H.1    Park, Y.C.2    Kreishman, M.3    Kieff, E.4    Wu, H.5
  • 26
    • 25444478027 scopus 로고    scopus 로고
    • ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation
    • Meulmeester E., Pereg Y., Shiloh Y., Jochemsen A.G. ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation. Cell Cycle 2005, 4:1166-1170.
    • (2005) Cell Cycle , vol.4 , pp. 1166-1170
    • Meulmeester, E.1    Pereg, Y.2    Shiloh, Y.3    Jochemsen, A.G.4
  • 27
    • 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
  • 28
    • 55449133376 scopus 로고    scopus 로고
    • Epstein-Barr nuclear antigen 1 contributes to nasopharyngeal carcinoma through disruption of PML nuclear bodies
    • Sivachandran N., Sarkari F., Frappier L. Epstein-Barr nuclear antigen 1 contributes to nasopharyngeal carcinoma through disruption of PML nuclear bodies. PLoS Pathog. 2008, 4:e1000170.
    • (2008) PLoS Pathog. , vol.4
    • Sivachandran, N.1    Sarkari, F.2    Frappier, L.3
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • Jones T.A., Kjeldgaard M. Electron-density map interpretation. Methods Enzymol. 1997, 277:173-208.
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.2
  • 33
    • 0036721834 scopus 로고    scopus 로고
    • The SPOT-synthesis technique. Synthetic peptide arrays on membrane supports-principles and applications
    • Frank R. The SPOT-synthesis technique. Synthetic peptide arrays on membrane supports-principles and applications. J. Immunol. Methods 2002, 267:13-26.
    • (2002) J. Immunol. Methods , vol.267 , pp. 13-26
    • Frank, R.1


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