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

页码：492 / 498

页数：7

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