Prolactin recruits STAT1, STAT3 and STAT5 independent of conserved receptor tyrosines TYR402, TYR479, TYR515 and TYR580. Mol Cell Endocrinol 1996 Mar 25;117(2):131-40
Date
03/25/1996Pubmed ID
8737372DOI
10.1016/0303-7207(95)03738-1Scopus ID
2-s2.0-0030000424 (requires institutional sign-in at Scopus site) 149 CitationsAbstract
The present study of prolactin (PRL) receptor-mediated recruitment of signal transducers and activators of transcription (STATs) demonstrates that PRL activates STAT3, in addition to STAT1 and STAT5 as previously reported, and that STAT1, STAT3 and STAT5 are mediators of PRL effects in cells whether of lymphoid, myeloid or mammary epithelial origin. Furthermore, receptor mutants M240 and T280 that do not mediate PRL-induced JAK2 activation and cell proliferation, are also unable to mediate STAT activation, supporting the proposed model of JAK2 as the initial effector protein used by PRL receptors. On the other hand, tyrosine phosphorylation analysis and electrophoretic mobility shift assays showed that receptor mutant G328, which lacks four of the five conserved cytoplasmic tyrosine residues of PRL receptors, retained the ability to activate JAK2 and STAT1, STAT3 and STAT5. These results support the notion that phosphotyrosyl residues other than those of the receptor, i.e., JAK2, are involved in recruiting STAT proteins to the activated PRL receptor complex.
Author List
DaSilva L, Rui H, Erwin RA, Howard OM, Kirken RA, Malabarba MG, Hackett RH, Larner AC, Farrar WLMESH terms used to index this publication - Major topics in bold
AnimalsBase Sequence
DNA-Binding Proteins
Humans
Mice
Milk Proteins
Molecular Sequence Data
Oligonucleotide Probes
Phosphorylation
Prolactin
Rats
Receptors, IgG
Receptors, Prolactin
STAT1 Transcription Factor
STAT3 Transcription Factor
STAT5 Transcription Factor
Sequence Deletion
Sheep
Time Factors
Trans-Activators
Tumor Cells, Cultured
Tyrosine
