Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response

被引：218

作者：

Reinhardt, H. Christian ^{[1
,2
,3
,4
]}

Yaffe, Michael B. ^{[1
,2
,5
]}

机构：

[1] MIT, Dept Biol, David H Koch Inst Integrat Canc Res, Cambridge, MA 02139 USA

[2] MIT, Dept Biol Engn, David H Koch Inst Integrat Canc Res, Cambridge, MA 02139 USA

[3] Univ Hosp Cologne, Ctr Internal Med, Div Hematol & Oncol, D-50937 Cologne, Germany

[4] Cluster Excellence Cellular Stress Responses Agin, Cologne, Germany

[5] Harvard Univ, Sch Med, Beth Israel Deaconess Med Ctr, Dept Surg, Boston, MA 02215 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2013年 / 14卷 / 09期

基金：

美国国家卫生研究院;

关键词：

POLO-LIKE KINASE-1; PEPTIDYL-PROLYL ISOMERASE; REPLICATION CHECKPOINT RESPONSE; SCF UBIQUITIN-LIGASE; DOUBLE-STRAND BREAKS; CHK2; PROTEIN-KINASE; S-PHASE CHECKPOINT; F-BOX PROTEINS; STRUCTURAL BASIS; FHA DOMAIN;

D O I：

10.1038/nrm3640

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Coordinated progression through the cell cycle is a complex challenge for eukaryotic cells. Following genotoxic stress, diverse molecular signals must be integrated to establish checkpoints specific for each cell cycle stage, allowing time for various types of DNA repair. Phospho-Ser/Thr-binding domains have emerged as crucial regulators of cell cycle progression and DNA damage signalling. Such domains include 14-3-3 proteins, WW domains, Polo-box domains (in PLK1), WD40 repeats (including those in the E3 ligase SCF beta TrCP), BRCT domains (including those in BRCA1) and FHA domains (such as in CHK2 and MDC1). Progress has been made in our understanding of the motif (or motifs) that these phospho-Ser/Thr-binding domains connect with on their targets and how these interactions influence the cell cycle and DNA damage response.

引用

页码：563 / 580

页数：18

共 248 条

[1] Normalization of nomenclature for peptide motifs as ligands of modular protein domains [J].