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Prlr binds Stat5
Stable Identifier
R-RNO-1369093
Type
Reaction [binding]
Species
Rattus norvegicus
Compartment
cytosol
,
plasma membrane
ReviewStatus
5/5
General
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PRLRs contain intracellular phosphorylated tyrosine residues that are able to bind and activate STATs, demonstrated by the co-immunoprecipitation of rat Prlr and Stat5 inPrlr mutants with a single intracellular tyrosine (Pezet et al. 1997). Prlr mutants with a single tyrosine residue at positions 599, 498 or 492 (reported as 580, 479 or 473 in Pezet et al. 1997) were all able to activate Stat5; Y599 gave a much stronger response. Short forms or Prlr lacking these tyrosines did not bind Stat5. Activation of Stat1 and Stat3 by Prlr has been reported (Da Silva et al. 1996) but the interaction has been suggested to be indirect and possibly mediated by Jak2.
Literature References
PubMed ID
Title
Journal
Year
9312112
Tyrosine docking sites of the rat prolactin receptor required for association and activation of stat5
Ferrag, F
,
Edery, M
,
Kelly, PA
,
Pezet, A
J Biol Chem
1997
Participants
Input
Prlr ligands:p(Y599)-Prlr:p(Y1007)-Jak2 dimer [plasma membrane]
(Rattus norvegicus)
Stat5 [cytosol]
(Rattus norvegicus)
Output
Prlr ligands:p(Y599)-Prlr:p(Y1007)-Jak2 dimer:Stat5 [plasma membrane]
(Rattus norvegicus)
Orthologous Events
PRLR binds STAT5 (Homo sapiens)
Authored
Jupe, S (2011-06-13)
Reviewed
Goffin, V (2011-11-08)
Created
Jupe, S (2011-07-04)
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