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Stimulation of the prolactin receptor (PRLr) with ligand
activates multiple kinase cascades. The proximal mediators involved in
the activation of the PRL-activated Raf-1 cascade in T-cells, however,
remain poorly characterized. The role of one proximal signaling
protein, namely p95
Volume 270,
Number 22,
Issue of June 2, pp. 13246-13253, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
, during PRLr signal
transduction was examined in the Nb2 T-cell line. The novel results
obtained here indicate that Vav is transiently associated with the PRLr
and is necessary for PRL-stimulated proliferation. During PRL
stimulation, a rapid and dramatic increase in guanine nucleotide
exchange factor (GEF) activity was found to be associated with Vav
immunoprecipitates. Concomitantly, an increase in Vav phosphorylation
on serine-threonine residues was observed. The Vav-associated GEF
activation could be inhibited by staurosporine and calphostin, but not
herbimycin, suggesting a modulatory role for phosphorylation at
serine-threonine residues. Treatment of Nb2 cells with antisense Vav
oligonucleotide ablated Vav expression and blocked PRL-driven
proliferation, but failed to inhibit PRL-induced GEF activation within
Nb2 lysates. These data indicate that GEF activity may not be intrinsic
to Vav as has been previously suggested, but either resides in or is
complemented by an associated GEF. Subsequent to the transient
activation of associated GEF activity, Vav was found to translocate
into the Nb2 cell nucleus. Thus, Vav may utilize two independent
mechanisms in T-cells, namely the activation of an associated GEF and
direct nuclear internalization, to mediate PRLr signaling.
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