Regulation of DNA repair by ubiquitylation

被引：214

作者：

Huang, TT

D'Andrea, AD

机构：

[1] Harvard Univ, Sch Med, Dana Farber Canc Inst, Dept Radiat Oncol, Boston, MA 02115 USA

[2] Harvard Univ, Sch Med, Dana Farber Canc Inst, Dept Pediat Oncol, Boston, MA 02115 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2006年 / 7卷 / 05期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1038/nrm1908

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The process of ubiquitylation is best known for its role in targeting proteins for degradation by the proteasome. However, recent studies of DNA-repair and DNA-damage-response pathways have significantly broadened the scope of the role of ubiquitylation to include non-proteolytic functions of ubiquitin. These pathways involve the monoubiquitylation of key DNA-repair proteins that have regulatory functions in homologous recombination and translesion DNA synthesis, and involve the polyubiquitylation of nucleotide-excision-repair proteins.

引用

收藏

页码：323 / 334

页数：12

相关论文

共 105 条

[41] Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways [J].

Hussain, S ;

Wilson, JB ;

Medhurst, AL ;

Hejna, J ;

Witt, E ;

Ananth, S ;

Davies, A ;

Masson, JY ;

Moses, R ;

West, SC ;

de Winter, JP ;

Ashworth, A ;

Jones, NJ ;

Mathew, CG .

HUMAN MOLECULAR GENETICS, 2004, 13 (12) :1241-1248

[42] BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression [J].

Jensen, DE ;

Proctor, M ;

Marquis, ST ;

Gardner, HP ;

Ha, SI ;

Chodosh, LA ;

Ishov, AM ;

Tommerup, N ;

Vissing, H ;

Sekido, Y ;

Minna, J ;

Borodovsky, A ;

Schultz, DC ;

Wilkinson, KD ;

Maul, GG ;

Barlev, N ;

Berger, SL ;

Prendergast, GC ;

Rauscher, FJ .

ONCOGENE, 1998, 16 (09) :1097-1112

[43] Protein modification by SUMO [J].

Johnson, ES .

ANNUAL REVIEW OF BIOCHEMISTRY, 2004, 73 :355-382

[44] Ubiquitin branches out [J].

Johnson, ES .

NATURE CELL BIOLOGY, 2002, 4 (12) :E295-E298

[45] Domain structure, localization, and function of DNA polymerase η, defective in xeroderma pigmentosum variant cells [J].

Kannouche, P ;

Broughton, BC ;

Volker, M ;

Hanaoka, F ;

Mullenders, LHF ;

Lehmann, AR .

GENES & DEVELOPMENT, 2001, 15 (02) :158-172

[46]

Kannouche PL, 2004, CELL CYCLE, V3, P1011

[47] Interaction of human DNA polymerase η with monoubiquitinated PCNA:: A possible mechanism for the polymerase switch in response to DNA damage [J].

Kannouche, PL ;

Wing, J ;

Lehmann, AR .

MOLECULAR CELL, 2004, 14 (04) :491-500

[48] The Fanconi Anemia/BRCA pathway: new faces in the crowd [J].

Kennedy, RD ;

D'Andrea, AD .

GENES & DEVELOPMENT, 2005, 19 (24) :2925-2940

[49] BRCA1/BARD1 inhibition of mRNA 3′ processing involves targeted degradation of RNA polymerase II [J].

Kleiman, FE ;

Wu-Baer, F ;

Fonseca, D ;

Kaneko, S ;

Baer, R ;

Manley, JL .

GENES & DEVELOPMENT, 2005, 19 (10) :1227-1237

[50] Ubiquitin/SUMO modification of PCNA promotes replication fork progression in Xenopus laevis egg extracts [J].

Leach, CA ;

Michael, WM .

JOURNAL OF CELL BIOLOGY, 2005, 171 (06) :947-954

← 1 2 3 4 5 6 7 8 9 10 →