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(Received for publication, May 29, 1997, and in revised form, July 16, 1997)
From INSERM U344-Endocrinologie Moléculaire, Faculté de
Medecine Necker Enfants Malades, 156 rue de Vaugirard,
75730 Paris Cedex 15, France
Prolactin (PRL) interacts with a single chain
prolactin-specific receptor of the cytokine receptor superfamily. PRL
triggers activation of Jak2 kinase which phosphorylates the PRL
receptor itself and the mammary gland factor, Stat5, a member of the
family of signal transducers and activators of transcription (Stat). Selection of the particular substrate (Stat 5), that is characterized by transcriptional responses to PRL, has been shown to be determined by
specific tyrosine-based motifs common to many cytokine receptors. PRL-induced activation of Stat5 was abolished in 293 fibroblasts expressing PRL receptor mutants lacking all intracellular tyrosines. We
have identified tyrosine phosphorylation sites of the PRL receptor (residues 580, 479, and 473) necessary for maximal Stat5 activation and
subsequent Stat5-dependent gene transcription. Moreover, we have shown that none of the tyrosine residues of the PRL receptor are
implicated in activation of Jak2. This study demonstrates that only
specific tyrosines in the PRL receptor are phosphorylated and are in
fact utilized differentially for Stat5-mediated transcriptional signaling.
Volume 272, Number 40,
Issue of October 3, 1997
pp. 25043-25050
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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