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The mammary factor MPBF is a prolactin‐induced transcriptional regulator which binds to STAT factor recognition sites
Author(s) -
Burdon Thomas G.,
Demmer Jerome,
Clark A.John,
Watson Christine J.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00757-8
Subject(s) - stat4 , transcription factor , microbiology and biotechnology , stat1 , binding site , prolactin , tyrosine phosphorylation , activator (genetics) , biology , phosphorylation , chemistry , stat , stat3 , biochemistry , gene , hormone
Site‐directed mutagenesis of the three binding sites for the mammary factor MPBF in the β‐lactoglobulin (BLG) promoter demonstrates that MPBF is a transcriptional activator of the BLG gene in mammary cells. MPBF requires phosphorylation on tyrosine for maximum binding activity and binds to GAS (interferon γ‐activation site) elements which are similar to the MPBF binding sites. Prolactin induces MPBF binding activity in CHO cells and is not antigenically related to Stat1 (p91) and Stat2 (p113), suggesting that this transcription factor is likely to be another member of the STAT family of cytokine/growth factor‐induced transcription factors.