Serine phosphorylation of STATs
Serine phosphorylation of STATs
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DOI：
10.1038/sj.onc.1203481
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发表时间：
2000-05-15
期刊：
影响因子：
8
通讯作者：
Kovarik, P
中科院分区：
文献类型：
--
作者：
Decker, T;Kovarik, P
酪氨酸磷酸化调节 STAT 的二聚化，这是建立经典 JAK-STAT 信号通路的重要先决条件。然而，大多数脊椎动物 STAT 在其 C 末端含有第二个磷酸化位点。在这种情况下，磷酸化残基是 P(M)SP 基序中包含的丝氨酸，并且在大多数情况下，其突变为丙氨酸会改变转录因子活性。这篇综述讨论了理解 STAT 丝氨酸磷酸化调节以及该过程中隐含的激酶和其他信号转导器的最新进展。讨论了 STAT 丝氨酸磷酸化的生化和生物学后果。
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.