Serine phosphorylation of STATs

被引：703

作者：

Decker, T ^{[1
]}

Kovarik, P ^{[1
]}

机构：

[1] Vienna Bioctr, Inst Microbiol & Genet, A-1030 Vienna, Austria

来源：

ONCOGENE | 2000年 / 19卷 / 21期

基金：

奥地利科学基金会;

关键词：

STAT; signal transduction; phosphorylation; MAP kinase;

D O I：

10.1038/sj.onc.1203481

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：

Tyrosine phosphorylation regulates the dimerization of STATs as an essential prerequisite for the establishment of a classical JAK-STAT signaling path. However, most vertebrate STATs contain a second phosphorylation site within their C-termini, The phosphorylated residue in this case is a serine contained within a P(M)SP motif, and in the majority of situations its mutation to alanine alters transcription factor activity. This review addresses recent advances in understanding the regulation of STAT serine phosphorylation, as well as the kinases and other signal transducers implied in this process. The biochemical and biological consequences of STAT serine phosphorylation are discussed.

引用

页码：2628 / 2637

页数：10

共 74 条

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