Dimerization in MAP-kinase signaling

被引：128

作者：

Cobb, MH

Goldsmith, EJ

机构：

[1] Univ Texas, SW Med Ctr, Dept Pharmacol, Dallas, TX 75235 USA

[2] Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75235 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2000年 / 25卷 / 01期

关键词：

D O I：

10.1016/S0968-0004(99)01508-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The stimulus-dependent nuclear localization of the extracellular-signal-regulated kinases ERK1 and ERK2 is required for many of their actions, including induction of neurites in PC12 cells and transformation of fibroblasts. Phosphorylation of ERK2 causes it to form dimers, and the most flexible portions of the ERK2 molecule provide the surfaces for dimerization. It is thought that dimerization promotes nuclear localization of ERK2 by its effects on import, export or retention in cytoplasmic and nuclear compartments. Dimerization might also influence substrate interactions.

引用

页码：7 / 9

页数：3

共 28 条

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