메뉴 건너뛰기




Volumn 44, Issue 1, 2011, Pages 147-159

Mechanism of USP7/HAUSP activation by its C-Terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE PHOSPHATE SYNTHETASE; PROTEINASE; SYNTHETASE; UBIQUITIN; UBIQUITIN SPECIFIC PROTEASE 7; UNCLASSIFIED DRUG;

EID: 80053594090     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2011.06.034     Document Type: Article
Times cited : (192)

References (50)
  • 2
    • 44349179787 scopus 로고    scopus 로고
    • A role of HAUSP in tumor suppression in a human colon carcinoma xenograft model
    • Becker K., Marchenko N.D., Palacios G., Moll U.M. A role of HAUSP in tumor suppression in a human colon carcinoma xenograft model. Cell Cycle 2008, 7:1205-1213.
    • (2008) Cell Cycle , vol.7 , pp. 1205-1213
    • Becker, K.1    Marchenko, N.D.2    Palacios, G.3    Moll, U.M.4
  • 4
    • 0019523261 scopus 로고
    • Guanosine-5'-phosphate synthetase and guanosine-5'-phosphate kinase in rat hepatomas and kidney tumors
    • Boritzki T.J., Jackson R.C., Morris H.P., Weber G. Guanosine-5'-phosphate synthetase and guanosine-5'-phosphate kinase in rat hepatomas and kidney tumors. Biochim. Biophys. Acta 1981, 658:102-110.
    • (1981) Biochim. Biophys. Acta , vol.658 , pp. 102-110
    • Boritzki, T.J.1    Jackson, R.C.2    Morris, H.P.3    Weber, G.4
  • 5
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
    • Borodovsky A., Kessler B.M., Casagrande R., Overkleeft H.S., Wilkinson K.D., Ploegh H.L. A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. EMBO J. 2001, 20:5187-5196.
    • (2001) EMBO J. , vol.20 , pp. 5187-5196
    • Borodovsky, A.1    Kessler, B.M.2    Casagrande, R.3    Overkleeft, H.S.4    Wilkinson, K.D.5    Ploegh, H.L.6
  • 6
    • 34548154812 scopus 로고    scopus 로고
    • Small but versatile: the extraordinary functional and structural diversity of the beta-grasp fold
    • Burroughs A.M., Balaji S., Iyer L.M., Aravind L. Small but versatile: the extraordinary functional and structural diversity of the beta-grasp fold. Biol. Direct 2007, 2:18.
    • (2007) Biol. Direct , vol.2 , pp. 18
    • Burroughs, A.M.1    Balaji, S.2    Iyer, L.M.3    Aravind, L.4
  • 7
    • 4644352805 scopus 로고    scopus 로고
    • A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7
    • Canning M., Boutell C., Parkinson J., Everett R.D. A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7. J. Biol. Chem. 2004, 279:38160-38168.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38160-38168
    • Canning, M.1    Boutell, C.2    Parkinson, J.3    Everett, R.D.4
  • 8
    • 3242774545 scopus 로고    scopus 로고
    • HAUSP is required for p53 destabilization
    • Cummins J.M., Vogelstein B. HAUSP is required for p53 destabilization. Cell Cycle 2004, 3:689-692.
    • (2004) Cell Cycle , vol.3 , pp. 689-692
    • Cummins, J.M.1    Vogelstein, B.2
  • 10
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. 2004, 60:2126-2132.
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 12
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P. Scaling and assessment of data quality. Acta Crystallogr. 2006, 62:72-82.
    • (2006) Acta Crystallogr. , vol.62 , pp. 72-82
    • Evans, P.1
  • 13
    • 34547799647 scopus 로고    scopus 로고
    • Biochemical characterization of USP7 reveals post-translational modification sites and structural requirements for substrate processing and subcellular localization
    • Fernandez-Montalvan A., Bouwmeester T., Joberty G., Mader R., Mahnke M., Pierrat B., Schlaeppi J.M., Worpenberg S., Gerhartz B. Biochemical characterization of USP7 reveals post-translational modification sites and structural requirements for substrate processing and subcellular localization. FEBS J. 2007, 274:4256-4270.
    • (2007) FEBS J. , vol.274 , pp. 4256-4270
    • Fernandez-Montalvan, A.1    Bouwmeester, T.2    Joberty, G.3    Mader, R.4    Mahnke, M.5    Pierrat, B.6    Schlaeppi, J.M.7    Worpenberg, S.8    Gerhartz, B.9
  • 14
    • 65249166493 scopus 로고    scopus 로고
    • Functional roles of ubiquitin-like domain (ULD) and ubiquitin-binding domain (UBD) containing proteins
    • Grabbe C., Dikic I. Functional roles of ubiquitin-like domain (ULD) and ubiquitin-binding domain (UBD) containing proteins. Chem. Rev. 2009, 109:1481-1494.
    • (2009) Chem. Rev. , vol.109 , pp. 1481-1494
    • Grabbe, C.1    Dikic, I.2
  • 16
    • 0036311587 scopus 로고    scopus 로고
    • USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product
    • Hong S., Kim S.J., Ka S., Choi I., Kang S. USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product. Mol. Cell. Neurosci. 2002, 20:298-306.
    • (2002) Mol. Cell. Neurosci. , vol.20 , pp. 298-306
    • Hong, S.1    Kim, S.J.2    Ka, S.3    Choi, I.4    Kang, S.5
  • 17
    • 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., Li W., Yao T., Wu J.W., Gu W., Cohen R.E., Shi Y. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 2002, 111:1041-1054.
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 18
    • 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. 10.1371/journal.pbio.0040027.
    • (2006) PLoS Biol. , vol.4
    • Hu, M.1    Gu, L.2    Li, M.3    Jeffrey, P.D.4    Gu, W.5    Shi, Y.6
  • 19
    • 67651151100 scopus 로고    scopus 로고
    • Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core
    • Khoo K.H., Joerger A.C., Freund S.M., Fersht A.R. Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core. Protein Eng. Des. Sel. 2009, 22:421-430.
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 421-430
    • Khoo, K.H.1    Joerger, A.C.2    Freund, S.M.3    Fersht, A.R.4
  • 20
    • 77952519938 scopus 로고    scopus 로고
    • Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module
    • Kohler A., Zimmerman E., Schneider M., Hurt E., Zheng N. Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module. Cell 2010, 141:606-617.
    • (2010) Cell , vol.141 , pp. 606-617
    • Kohler, A.1    Zimmerman, E.2    Schneider, M.3    Hurt, E.4    Zheng, N.5
  • 21
    • 39549106692 scopus 로고    scopus 로고
    • The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module
    • Komander D., Lord C.J., Scheel H., Swift S., Hofmann K., Ashworth A., Barford D. The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module. Mol. Cell 2008, 29:451-464.
    • (2008) Mol. Cell , vol.29 , pp. 451-464
    • Komander, D.1    Lord, C.J.2    Scheel, H.3    Swift, S.4    Hofmann, K.5    Ashworth, A.6    Barford, D.7
  • 23
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. 2004, 60:2256-2268.
    • (2004) Acta Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 24
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer G., Cohen S.X., Lamzin V.S., Perrakis A. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 2008, 3:1171-1179.
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 26
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie A.G. The integration of macromolecular diffraction data. Acta Crystallogr. 2006, 62:48-57.
    • (2006) Acta Crystallogr. , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 27
    • 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
  • 28
    • 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
  • 32
    • 33847276654 scopus 로고    scopus 로고
    • Monoubiquitylation promotes mitochondrial p53 translocation
    • Marchenko N.D., Wolff S., Erster S., Becker K., Moll U.M. Monoubiquitylation promotes mitochondrial p53 translocation. EMBO J. 2007, 26:923-934.
    • (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
  • 35
    • 77953060092 scopus 로고    scopus 로고
    • Structural insights into the assembly and function of the SAGA deubiquitinating module
    • Samara N.L., Datta A.B., Berndsen C.E., Zhang X., Yao T., Cohen R.E., Wolberger C. Structural insights into the assembly and function of the SAGA deubiquitinating module. Science 2010, 328:1025-1029.
    • (2010) Science , vol.328 , pp. 1025-1029
    • Samara, N.L.1    Datta, A.B.2    Berndsen, C.E.3    Zhang, X.4    Yao, T.5    Cohen, R.E.6    Wolberger, C.7
  • 36
    • 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., Zhang R.G., Liao J., Lee W., Edwards A.M., 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    Zhang, R.G.7    Liao, J.8    Lee, W.9    Edwards, A.M.10
  • 37
    • 73449097872 scopus 로고    scopus 로고
    • EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication
    • Sarkari F., Sanchez-Alcaraz T., Wang S., Holowaty M.N., Sheng Y., Frappier L. EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication. PLoS Pathog. 2009, 5:e1000624. 10.1371/journal.ppat.1000624.
    • (2009) PLoS Pathog. , vol.5
    • Sarkari, F.1    Sanchez-Alcaraz, T.2    Wang, S.3    Holowaty, M.N.4    Sheng, Y.5    Frappier, L.6
  • 38
    • 77958566202 scopus 로고    scopus 로고
    • USP7/HAUSP promotes the sequence-specific DNA binding activity of p53
    • Sarkari F., Sheng Y., Frappier L. USP7/HAUSP promotes the sequence-specific DNA binding activity of p53. PLoS ONE 2010, 5:e13040. 10.1371/journal.pone.0013040.
    • (2010) PLoS ONE , vol.5
    • Sarkari, F.1    Sheng, Y.2    Frappier, L.3
  • 40
    • 78651482046 scopus 로고    scopus 로고
    • Nuclear PTEN regulates the APC-CDH1 tumor-suppressive complex in a phosphatase-independent manner
    • Song M.S., Carracedo A., Salmena L., Song S.J., Egia A., Malumbres M., Pandolfi P.P. Nuclear PTEN regulates the APC-CDH1 tumor-suppressive complex in a phosphatase-independent manner. Cell 2011, 144:187-199.
    • (2011) Cell , vol.144 , pp. 187-199
    • Song, M.S.1    Carracedo, A.2    Salmena, L.3    Song, S.J.4    Egia, A.5    Malumbres, M.6    Pandolfi, P.P.7
  • 41
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa M.E., Bennett E.J., Gygi S.P., Harper J.W. 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
  • 42
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun D.I., Petoukhov M.V., Koch M.H. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 2001, 80:2946-2953.
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 46
    • 75149157727 scopus 로고    scopus 로고
    • Biosynthetic enzyme GMP synthetase cooperates with ubiquitin-specific protease 7 in transcriptional regulation of ecdysteroid target genes
    • van der Knaap J.A., Kozhevnikova E., Langenberg K., Moshkin Y.M., Verrijzer C.P. Biosynthetic enzyme GMP synthetase cooperates with ubiquitin-specific protease 7 in transcriptional regulation of ecdysteroid target genes. Mol. Cell. Biol. 2010, 30:736-744.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 736-744
    • van der Knaap, J.A.1    Kozhevnikova, E.2    Langenberg, K.3    Moshkin, Y.M.4    Verrijzer, C.P.5
  • 49
    • 0020656145 scopus 로고
    • Purine and pyrimidine enzymic programs and nucleotide pattern in sarcoma
    • Weber G., Burt M.E., Jackson R.C., Prajda N., Lui M.S., Takeda E. Purine and pyrimidine enzymic programs and nucleotide pattern in sarcoma. Cancer Res. 1983, 43:1019-1023.
    • (1983) Cancer Res. , vol.43 , pp. 1019-1023
    • Weber, G.1    Burt, M.E.2    Jackson, R.C.3    Prajda, N.4    Lui, M.S.5    Takeda, E.6
  • 50
    • 34548354844 scopus 로고    scopus 로고
    • High incidence of ubiquitin-like domains in human ubiquitin-specific proteases
    • Zhu X., Menard R., Sulea T. High incidence of ubiquitin-like domains in human ubiquitin-specific proteases. Proteins 2007, 69:1-7.
    • (2007) Proteins , vol.69 , pp. 1-7
    • Zhu, X.1    Menard, R.2    Sulea, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.