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Papers In Press, published online ahead of print March 5, 2003
Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030-3498
Corresponding Author: jrosen{at}bcm.tmc.edu
Stat5 is activated by a broad spectrum of cytokines, as well as non-receptor tyrosine kinases, such as Src. In this study, the DNA-binding properties of the two closely related Stat5 proteins, Stat5a and Stat5b, induced either by Prl or by Src were analyzed by electrophoretic mobility shift assays using several different Stat5 binding sites. Src-induced Stat5b DNA-binding complexes consistently displayed a slightly faster mobility than those induced by Prl, as well as differences in their ability to be supershifted by anti-Stat5 antibodies. IP-Westerns performed using specific antibodies directed at the N- and C-termini of Stat5b suggested that depending on the activating stimulus, Stat5b exhibited different conformations, which influenced antibody accessibility at its C-terminus. These conformational differences may in part be due to differential effects of Prl and Src on Stat5b tyrosine phosphorylation, since Src induced several additional sites of tyrosine phosphorylation of Stat5b at residues other than Y699, including Y724 and Y679. The latter Y679 is conserved in all mammalian Stat5b's, but is not present in Stat5a. A Stat 5bY679F mutant induced by Src kinase exhibited an altered pattern of nuclear localization as compared to wild type Stat5b. Furthermore, this mutation inhibited v-Src-induced cyclin D1-luciferase reporter activity in transient transfection assays performed in Stat5a/b-deficient MEFs, suggesting that Y679 phosphorylation may play a role in v-Src induced proliferation. Thus, depending on the signal transduction pathway responsible for activation, different conformations of activated Stat5 may result in selective biological responses.
J. Biol. Chem, 10.1074/jbc.M301578200
Submitted on February 13, 2003
Revised on March 5, 2003
Accepted on March 4, 2003
Signal transduction pathways regulated by prolactin and Src result in different conformations of activated Stat5b
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