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Volumn 289, Issue 39, 2014, Pages 27278-27289

Ubiquitin-specific Protease 7 Regulates Nucleotide Excision Repair through Deubiquitinating XPC Protein and Preventing XPC Protein from Undergoing Ultraviolet Light-induced and VCP/p97 Protein-regulated Proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

LIGHT-INDUCED; NUCLEOTIDE EXCISION REPAIR;

EID: 84907478478     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.589812     Document Type: Article
Times cited : (75)

References (43)
  • 1
    • 0033118354 scopus 로고    scopus 로고
    • Molecular mechanism of nucleotide excision repair
    • de Laat, W. L., Jaspers, N. G., and Hoeijmakers, J. H. (1999) Molecular mechanism of nucleotide excision repair. Genes Dev. 13, 768-785
    • (1999) Genes Dev , vol.13 , pp. 768-785
    • De Laat, W.L.1    Jaspers, N.G.2    Hoeijmakers, J.H.3
  • 2
    • 0031060362 scopus 로고    scopus 로고
    • Role of DNA excision repair gene defects in the etiology of cancer
    • Ford, J. M., and Hanawalt, P. C. (1997) Role of DNA excision repair gene defects in the etiology of cancer. Curr. Top. Microbiol. Immunol. 221, 47-70
    • (1997) Curr. Top. Microbiol. Immunol , vol.221 , pp. 47-70
    • Ford, J.M.1    Hanawalt, P.C.2
  • 3
    • 0025775473 scopus 로고
    • Xeroderma pigmentosum complementation group C cells remove pyrimidine dimers selectively from the transcribed strand of active genes
    • Venema, J., van Hoffen, A., Karcagi, V., Natarajan, A. T., van Zeeland, A. A., and Mullenders, L. H. (1991) Xeroderma pigmentosum complementation group C cells remove pyrimidine dimers selectively from the transcribed strand of active genes. Mol. Cell Biol. 11, 4128-4134
    • (1991) Mol. Cell Biol , vol.11 , pp. 4128-4134
    • Venema, J.1    Van Hoffen, A.2    Karcagi, V.3    Natarajan, A.T.4    Van Zeeland, A.A.5    Mullenders, L.H.6
  • 4
    • 0035374836 scopus 로고    scopus 로고
    • Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair
    • Araki, M., Masutani, C., Takemura, M., Uchida, A., Sugasawa, K., Kondoh, J., Ohkuma, Y., and Hanaoka, F. (2001) Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. J. Biol. Chem. 276, 18665-18672
    • (2001) J. Biol. Chem , vol.276 , pp. 18665-18672
    • Araki, M.1    Masutani, C.2    Takemura, M.3    Uchida, A.4    Sugasawa, K.5    Kondoh, J.6    Ohkuma, Y.7    Hanaoka, F.8
  • 6
    • 0027964775 scopus 로고
    • DNA repair defect in xeroderma pigmentosum group C and complementing factor from HeLa cells
    • Shivji, M. K., Eker, A. P., and Wood, R. D. (1994) DNA repair defect in xeroderma pigmentosum group C and complementing factor from HeLa cells. J. Biol. Chem. 269, 22749-22757
    • (1994) J. Biol. Chem , vol.269 , pp. 22749-22757
    • Shivji, M.K.1    Eker, A.P.2    Wood, R.D.3
  • 7
    • 0036012799 scopus 로고    scopus 로고
    • A molecular mechanism forDNAdamage recognition by the xeroderma pigmentosum group C protein complex
    • Sugasawa, K., Shimizu, Y., Iwai, S., and Hanaoka, F. (2002) A molecular mechanism forDNAdamage recognition by the xeroderma pigmentosum group C protein complex. DNA Repair 1, 95-107
    • (2002) DNA Repair , vol.1 , pp. 95-107
    • Sugasawa, K.1    Shimizu, Y.2    Iwai, S.3    Hanaoka, F.4
  • 8
    • 84887164461 scopus 로고    scopus 로고
    • Xeroderma pigmentosum complementation group C protein (XPC) serves as a general sensor of damaged DNA
    • Shell, S. M., Hawkins, E. K., Tsai, M. S., Hlaing, A. S., Rizzo, C. J., and Chazin, W. J. (2013) Xeroderma pigmentosum complementation group C protein (XPC) serves as a general sensor of damaged DNA. DNA Repair 12, 947-953
    • (2013) DNA Repair , vol.12 , pp. 947-953
    • Shell, S.M.1    Hawkins, E.K.2    Tsai, M.S.3    Hlaing, A.S.4    Rizzo, C.J.5    Chazin, W.J.6
  • 9
    • 0023803543 scopus 로고
    • Xeroderma pigmentosum group e cells lack a nuclear factor that binds to damaged DNA
    • Chu, G., and Chang, E. (1988) Xeroderma pigmentosum group E cells lack a nuclear factor that binds to damaged DNA. Science 242, 564-567
    • (1988) Science , vol.242 , pp. 564-567
    • Chu, G.1    Chang, E.2
  • 10
    • 0000516293 scopus 로고    scopus 로고
    • Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair
    • Hwang, B. J., Ford, J. M., Hanawalt, P. C., and Chu, G. (1999) Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair. Proc. Natl. Acad. Sci. U.S.A. 96, 424-428
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 424-428
    • Hwang, B.J.1    Ford, J.M.2    Hanawalt, P.C.3    Chu, G.4
  • 11
    • 0029768095 scopus 로고    scopus 로고
    • Mutations specific to the xeroderma pigmentosum group e Ddb- phenotype
    • Nichols, A. F., Ong, P., and Linn, S. (1996) Mutations specific to the xeroderma pigmentosum group E Ddb- phenotype. J. Biol. Chem. 271, 24317-24320
    • (1996) J. Biol. Chem , vol.271 , pp. 24317-24320
    • Nichols, A.F.1    Ong, P.2    Linn, S.3
  • 12
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • Groisman, R., Polanowska, J., Kuraoka, I., Sawada, J., Saijo, M., Drapkin, R., Kisselev, A. F., Tanaka, K., and Nakatani, Y. (2003) The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 113, 357-367
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3    Sawada, J.4    Saijo, M.5    Drapkin, R.6    Kisselev, A.F.7    Tanaka, K.8    Nakatani, Y.9
  • 14
    • 22244478319 scopus 로고    scopus 로고
    • DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation
    • Wang, Q. E., Zhu, Q., Wani, G., El-Mahdy, M. A., Li, J., and Wani, A. A. (2005) DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation. Nucleic Acids Res. 33, 4023-4034
    • (2005) Nucleic Acids Res , vol.33 , pp. 4023-4034
    • Wang, Q.E.1    Zhu, Q.2    Wani, G.3    El-Mahdy, M.A.4    Li, J.5    Wani, A.A.6
  • 15
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander, D., Clague, M. J., and Urbé, S. (2009) Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 10, 550-563
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbé, S.3
  • 17
    • 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., and Gu, W. (2002) Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 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
  • 19
    • 0023425741 scopus 로고
    • Quantitation of pyrimidine dimers by immunoslot blot following sublethal UV-irradiation of human cells
    • Wani, A. A., D'Ambrosio, S. M., and Alvi, N. K. (1987) Quantitation of pyrimidine dimers by immunoslot blot following sublethal UV-irradiation of human cells. Photochem. Photobiol. 46, 477-482
    • (1987) Photochem. Photobiol , vol.46 , pp. 477-482
    • Wani, A.A.1    D'ambrosio, S.M.2    Alvi, N.K.3
  • 20
    • 35748950163 scopus 로고    scopus 로고
    • Damage-induced ubiquitylation of human RNA polymerase II by the ubiquitin ligase Nedd4, but not Cockayne syndrome proteins or BRCA1
    • Anindya, R., Aygün, O., and Svejstrup, J. Q. (2007) Damage-induced ubiquitylation of human RNA polymerase II by the ubiquitin ligase Nedd4, but not Cockayne syndrome proteins or BRCA1. Mol. Cell 28, 386-397
    • (2007) Mol. Cell , vol.28 , pp. 386-397
    • Anindya, R.1    Aygün, O.2    Svejstrup, J.Q.3
  • 21
    • 77955209543 scopus 로고    scopus 로고
    • Dissociation of CAK from core TFIIH reveals a functional link between XP-G/CS and the TFIIH disassembly state
    • Arab, H. H., Wani, G., Ray, A., Shah, Z. I., Zhu, Q., and Wani, A. A. (2010) Dissociation of CAK from core TFIIH reveals a functional link between XP-G/CS and the TFIIH disassembly state. PLoS ONE 5, e11007
    • (2010) PLoS ONE , vol.5 , pp. e11007
    • Arab, H.H.1    Wani, G.2    Ray, A.3    Shah, Z.I.4    Zhu, Q.5    Wani, A.A.6
  • 23
    • 84869815167 scopus 로고    scopus 로고
    • Identification of a functional in vivo p53 response element in the coding sequence of the xeroderma pigmentosum group C gene
    • Hastak, K., Adimoolam, S., Trinklein, N. D., Myers, R. M., and Ford, J. M. (2012) Identification of a functional in vivo p53 response element in the coding sequence of the xeroderma pigmentosum group C gene. Genes Cancer 3, 131-140
    • (2012) Genes Cancer , vol.3 , pp. 131-140
    • Hastak, K.1    Adimoolam, S.2    Trinklein, N.D.3    Myers, R.M.4    Ford, J.M.5
  • 24
    • 33744958177 scopus 로고    scopus 로고
    • Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites regulates in vivo lesion recognition by XPC
    • El-Mahdy, M. A., Zhu, Q., Wang, Q. E., Wani, G., Praetorius-Ibba, M., and Wani, A. A. (2006) Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites regulates in vivo lesion recognition by XPC. J. Biol. Chem. 281, 13404-13411
    • (2006) J. Biol. Chem , vol.281 , pp. 13404-13411
    • El-Mahdy, M.A.1    Zhu, Q.2    Wang, Q.E.3    Wani, G.4    Praetorius-Ibba, M.5    Wani, A.A.6
  • 26
    • 80053594090 scopus 로고    scopus 로고
    • Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase
    • Faesen, A. C., Dirac, A. M., Shanmugham, A., Ovaa, H., Perrakis, A., and Sixma, T. K. (2011) Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase. Mol. Cell 44, 147-159
    • (2011) Mol. Cell , vol.44 , pp. 147-159
    • Faesen, A.C.1    Dirac, A.M.2    Shanmugham, A.3    Ovaa, H.4    Perrakis, A.5    Sixma, T.K.6
  • 28
    • 84883506815 scopus 로고    scopus 로고
    • Put a RING on it: Regulation and inhibition of RNF8 and RNF168 RING finger E3 ligases at DNA damage sites
    • Bartocci, C., and Denchi, E. L. (2013) Put a RING on it: regulation and inhibition of RNF8 and RNF168 RING finger E3 ligases at DNA damage sites. Front Genet. 4, 128
    • (2013) Front Genet , vol.4 , pp. 128
    • Bartocci, C.1    Denchi, E.L.2
  • 32
    • 0038339144 scopus 로고    scopus 로고
    • A novel regulation mechanism ofDNArepair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein
    • Ng, J. M., Vermeulen, W., van der Horst, G. T., Bergink, S., Sugasawa, K., Vrieling, H., and Hoeijmakers, J. H. (2003) A novel regulation mechanism ofDNArepair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein. Genes Dev. 17, 1630-1645
    • (2003) Genes Dev , vol.17 , pp. 1630-1645
    • Ng, J.M.1    Vermeulen, W.2    Van Der Horst, G.T.3    Bergink, S.4    Sugasawa, K.5    Vrieling, H.6    Hoeijmakers, J.H.7
  • 33
    • 0033538572 scopus 로고    scopus 로고
    • Characterization of DNA recognition by the human UV-damaged DNA-binding protein
    • Fujiwara, Y., Masutani, C., Mizukoshi, T., Kondo, J., Hanaoka, F., and Iwai, S. (1999) Characterization of DNA recognition by the human UV-damaged DNA-binding protein. J. Biol. Chem. 274, 20027-20033
    • (1999) J. Biol. Chem , vol.274 , pp. 20027-20033
    • Fujiwara, Y.1    Masutani, C.2    Mizukoshi, T.3    Kondo, J.4    Hanaoka, F.5    Iwai, S.6
  • 34
    • 0037127293 scopus 로고    scopus 로고
    • DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair
    • Wakasugi, M., Kawashima, A., Morioka, H., Linn, S., Sancar, A., Mori, T., Nikaido, O., and Matsunaga, T. (2002) DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair. J. Biol. Chem. 277, 1637-1640
    • (2002) J. Biol. Chem , vol.277 , pp. 1637-1640
    • Wakasugi, M.1    Kawashima, A.2    Morioka, H.3    Linn, S.4    Sancar, A.5    Mori, T.6    Nikaido, O.7    Matsunaga, T.8
  • 36
    • 84861970930 scopus 로고    scopus 로고
    • P97 complexes as signal integration hubs
    • Meyer, H. (2012) p97 complexes as signal integration hubs. BMC. Biol. 10, 48
    • (2012) BMC. Biol , vol.10 , pp. 48
    • Meyer, H.1
  • 38
    • 78650733298 scopus 로고    scopus 로고
    • Cdc48/p97 mediates UV-dependent turnover of RNA Pol II
    • Verma, R., Oania, R., Fang, R., Smith, G. T., and Deshaies, R. J. (2011) Cdc48/p97 mediates UV-dependent turnover of RNA Pol II. Mol. Cell 41, 82-92
    • (2011) Mol. Cell , vol.41 , pp. 82-92
    • Verma, R.1    Oania, R.2    Fang, R.3    Smith, G.T.4    Deshaies, R.J.5
  • 39
    • 84899627951 scopus 로고    scopus 로고
    • Chromatin retention of DNA damage sensors DDB2 and XPC through loss of p97 segregase causes genotoxicity
    • Puumalainen, M. R., Lessel, D., Rüthemann, P., Kaczmarek, N., Bachmann, K., Ramadan, K., and Naegeli, H. (2014) Chromatin retention of DNA damage sensors DDB2 and XPC through loss of p97 segregase causes genotoxicity. Nat. Commun. 5, 3695
    • (2014) Nat. Commun , vol.5 , pp. 3695
    • Puumalainen, M.R.1    Lessel, D.2    Rüthemann, P.3    Kaczmarek, N.4    Bachmann, K.5    Ramadan, K.6
  • 40
    • 82955233157 scopus 로고    scopus 로고
    • The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks
    • Acs, K., Luijsterburg, M. S., Ackermann, L., Salomons, F. A., Hoppe, T., and Dantuma, N. P. (2011) The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks. Nat. Struct. Mol. Biol. 18, 1345-1350
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 1345-1350
    • Acs, K.1    Luijsterburg, M.S.2    Ackermann, L.3    Salomons, F.A.4    Hoppe, T.5    Dantuma, N.P.6
  • 42
  • 43
    • 80053583606 scopus 로고    scopus 로고
    • A genome- wide screen identifies p97 as an essential regulator of DNA damage- dependent CDT1 destruction
    • Raman, M., Havens, C. G., Walter, J. C., and Harper, J. W. (2011) A genome- wide screen identifies p97 as an essential regulator of DNA damage- dependent CDT1 destruction. Mol. Cell 44, 72-84.
    • (2011) Mol. Cell , vol.44 , pp. 72-84
    • Raman, M.1    Havens, C.G.2    Walter, J.C.3    Harper, J.W.4


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