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J Biol Chem, Vol. 274, Issue 32, 22484-22492, August 6, 1999
From the Department of Cell Biology, Baylor College of Medicine,
Houston, Texas 77030-3498
In this study, DNA binding and tyrosine
phosphorylation of STAT5A and STAT5B were compared with their
subcellular localization determined using indirect immunofluorescence
microscopy. Following prolactin activation, both STAT5A and STAT5B were
rapidly translocated into the nucleus and displayed a
detergent-resistant, punctate nuclear staining pattern. Similar to
prolactin induction, src activation resulted in tyrosine
phosphorylation and DNA binding of both STAT5A and STAT5B. However,
nuclear translocation of only STAT5B but not STAT5A was observed. This
selective nuclear translocation appears to be mediated via the
carboxyl-terminal sequences in STAT5B. Furthermore, overexpression of a
dominant negative kinase-inactive mutant of JAK2 prevented
prolactin-induced tyrosine phosphorylation and nuclear translocation of
STAT5A and STAT5B but did not block src kinase activation
and nuclear translocation of STAT5B. In co-transfection assays,
prolactin-mediated activation but not src kinase-mediated
activation of STAT5B resulted in the induction of a 
-casein
promoter-driven reporter construct. These results suggest that STAT5
activation by src may occur by a mechanism distinct from
that employed in cytokine activation of the JAK/STAT pathway, resulting
in the selective nuclear translocation of STAT5B.
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