Prlr-bound Stat5 is phosphorylated

Stable Identifier
R-RNO-1671699
Type
Reaction [transition]
Species
Rattus norvegicus
Compartment
General
SVG |   | PPTX  | SBGN
Prlr-bound Stat5 is phosphorylated

Co-immunoprecipitation of rat Prlr and Stat5 in mutated Prlrs having a single intracellular tyrosine suggests that phosphorylation of these tyrosines is required for Stat5 binding and leads to Stat5 tyrosine phosphorylation (Pezet et al. 1997). STAT1 and STAT3 have both been reported to be activated by PRLR (DaSilva et al. 1996), but the region(s) of PRLR required for activation of these Stats remains poorly documented.

Literature References
PubMed ID Title Journal Year
9312112 Tyrosine docking sites of the rat prolactin receptor required for association and activation of stat5

Pezet, A, Ferrag, F, Kelly, PA, Edery, M

J Biol Chem 1997
Participants
Orthologous Events
Authored
Reviewed
Created