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(Received for publication, August 9, 1996, and in revised form, November 20, 1996)
,
From the Prolactin (PRL) has been demonstrated to induce
tyrosine phosphorylation and activation of the cytoplasmic tyrosine
kinase JAK2. The present study represents an initial effort to identify the phosphorylation repertoire of the PRL receptor (PRLR). For this
purpose we have modified the rat PRLR cDNA to encode an additional N-terminal epitope specifically designed to allow the rapid
purification of the PRLR and associated proteins from transfected
cells. The Flag-tagged PRLR was stably expressed in the human 293 cell
line. PRL induced tyrosine phosphorylation of proteins of 85, 95, and 185 kDa from 10 to 30 min after PRL stimulation. Immunoblot analysis of
immunoprecipitation indicates that p85 corresponds to the 85-kDa regulatory subunit of phosphatidylinositol (PI)-3
Departamento de Biologia Molecular,
Universidad Autonoma de Madrid, Facultad de Ciencias, 28049 Madrid,
Spain, the § Dipartimento di Farmacologia Sperimentale,
Università degli Studi di Napoli "Federico II," 80131 Napoli,
Italy, and INSERM U.344, Endocrinologie Moléculaire,
Faculté de Médecine Necker, 75730 Paris Cedex 15, France
kinase, p95 to PRLR,
and p185 to insulin receptor substrate 1 (IRS-1). Both PI-3 kinase and
IRS-1 appear to associate with PRLR in a PRL-dependent manner. These results thus indicate that kinases other than JAK2, namely PI-3 kinase, are activated by PRL.
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