Coordination of cell growth and division by the ubiquitin-proteasome system

被引：36
作者：
Benanti, Jennifer A. [1 ,2 ]
机构：
[1] Univ Massachusetts, Sch Med, Program Gene Funct & Express, Worcester, MA 01605 USA
[2] Univ Massachusetts, Sch Med, Program Mol Med, Worcester, MA 01605 USA
来源：
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY | 2012年 / 23卷 / 05期
关键词：
Cell cycle; Ubiquitin; Proteolysis; Cyclin; Glycolysis; CYCLE-REGULATED GENES; PHOSPHORYLATION-DEPENDENT UBIQUITINATION; D1 NUCLEAR EXPORT; F-BOX PROTEINS; SACCHAROMYCES-CEREVISIAE; S-PHASE; CDK-INHIBITOR; MULTISITE PHOSPHORYLATION; GLUCOSE REPRESSION; DNA-DAMAGE;
D O I：
10.1016/j.semcdb.2012.04.005
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
The coupling of cellular growth and division is crucial for a cell to make an accurate copy of itself. Regulated protein degradation by the ubiquitin-proteasome system (UPS) plays an important role in the coordination of these two processes. Many ubiquitin ligases, in particular the Skp1-Cullin-F-box (SCF) family and the Anaphase-Promoting Complex (APC), couple growth and division by targeting cell cycle and metabolic regulators for degradation. However, many regulatory proteins are targeted by multiple ubiquitin ligases. As a result, we are only just beginning to understand the complexities of the proteolytic regulatory network that connects cell growth and the cell cycle. (c) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码：492 / 498
页数：7
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