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STAT1 — TYR
Text-mined interactions from Literome
Aittomäki et al., J Immunol 2000
:
The cooperation required phosphorylation of
Tyr701 , DNA binding, and the trans-activation domain of Stat1, but did not
involve Ser727 phosphorylation of
Stat1 or physical interaction between GR and Stat1
Mazière et al., Free Radic Biol Med 2001
:
Genistein, a nonspecific
Tyr-kinase inhibitor, and AG490, a specific inhibitor of JAKs, markedly
prevented the CuLDL induced enhancement of
STAT1 and STAT3 Tyr-phosphorylation and DNA binding activity, suggesting that JAKs are the main kinases involved in STATs ' activation by oxidized LDL
Qing et al., J Biol Chem 2005
:
Here we show that
Tyr ( 441 ) is
required to attenuate
STAT1 activation in response to IFNgamma
Zhang et al., J Biol Chem 2005
(Inflammation) :
Moreover,
Stat1-CC still
required ligand dependent
Tyr-701 phosphorylation for function and exhibited hyperresponsiveness to IFN-beta ( that depends on Stat1/Stat2 heterodimerization ) as well as IFN-gamma ( that depends on Stat1/Stat1 homodimerization )