Journal
ONCOGENE
Volume 19, Issue 21, Pages 2628-2637Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.onc.1203481
Keywords
STAT; signal transduction; phosphorylation; MAP kinase
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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.
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