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PTP1D is a positive regulator of the prolactin signal leading to beta‐casein promoter activation.
Author(s) -
Ali S.,
Chen Z.,
Lebrun J. J.,
Vogel W.,
Kharitonenkov A.,
Kelly P. A.,
Ullrich A.
Publication year - 1996
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1996.tb00341.x
Subject(s) - biology , regulator , prolactin , beta (programming language) , microbiology and biotechnology , genetics , endocrinology , hormone , gene , computer science , programming language
Stimulation of the prolactin receptor (PRLR), a member of the cytokine/growth hormone receptor family, results in activation of the associated Jak2 tyrosine kinase and downstream signaling pathways. We report that PTP1D, a cytoplasmic protein tyrosine phosphatase containing two Src homology 2 (SH2) domains, physically associates with the PRLR‐Jak2 complex and is tyrosine‐phosphorylated upon stimulation with prolactin. The formation of the trimeric PRLR‐Jak2‐PTP1D complex is critical for transmission of a lactogenic signal, while PTP1D phosphorylation is necessary, but not sufficient. The dominant negative inhibitory effect of a phosphatase‐deficient mutant on expression of a beta‐casein promoter‐controlled reporter gene is evidence for an essential role of fully functional PTP1D in the regulation of milk protein gene transcription.