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Serine phosphorylation of Stat5 proteins in lymphocytes stimulated with IL-2
Tyrosine phosphorylation regulates cytokine-induced dimerization of STAT proteins. Serine phosphorylation has also been found to occur in a number of STAT proteins, including Stat1, Sat3, Stat4, Stat5a, Stat5b and Stat6, and was shown to be important for maximal transcriptional activation mediated by Stat1, Stat3 and Stat4, but not for Stat5a or Stat5b. As these latter proteins were studied in transiently transfected COS-7 cells stimulated with prolactin, we sought to further investigate thedoi:10.1093/intimm/dxf101 pmid:12407017 fatcat:usrermazdjfqzhkbpcb6dzwbme