Serine phosphorylation of STATs
Open Access
- 25 May 2000
- journal article
- review article
- Published by Springer Science and Business Media LLC in Oncogene
- Vol. 19 (21), 2628-2637
- https://doi.org/10.1038/sj.onc.1203481
Abstract
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.Keywords
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