Atypical mitogen-activated protein kinases: Structure, regulation and functions

被引:214
作者
Coulombe, Phillipe
Meloche, Sylvain
机构
[1] Univ Montreal, Inst Rech Immunol & Cancerol, Montreal, PQ H3C 3J7, Canada
[2] Univ Montreal, Dept Pharmacol, Montreal, PQ H3C 3J7, Canada
[3] Univ Montreal, Dept Mol Biol, Montreal, PQ H3C 3J7, Canada
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2007年 / 1773卷 / 08期
基金
加拿大健康研究院;
关键词
protein phosphorylation; MAP kinase; extracellular signal regulated kinase; nemo-like kinase; structure; substrate specificity;
D O I
10.1016/j.bbamcr.2006.11.001
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
Mitogen-activated protein (MAP) kinases are a family of serine/threonine kinases that play a central role in transducing extracellular cues into a variety of intracellular responses ranging from lineage specification to cell division and adaptation. Fourteen MAP kinase genes have been identified in the human genome, which define 7 distinct MAP kinase signaling pathways. MAP kinases can be classified into conventional or atypical enzymes, based on their ability to get phosphorylated and activated by members of the MAP kinase kinase(MAPKK)/MEK family. Conventional MAP kinases comprise ERK1/ERK2, p38s, JNKs, and ERK5, which are all substrates of MAPKKs. Atypical MAP kinases include ERK3/ERK4, NLK and ERK7. Much less is known about the regulation, substrate specificity and physiological functions of atypical MAP kinases. (C) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:1376 / 1387
页数:12
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