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STAT3 — TYR
Text-mined interactions from Literome
Banks et al., J Biol Chem 2000
:
By using this system, we confirm that two tyrosine residues in the intracellular domain of murine LRb become phosphorylated to mediate LRb signaling ;
Tyr ( 985 ) controls the tyrosine phosphorylation of SHP-2, and Tyr ( 1138 )
controls STAT3 activation
Bjorbak et al., J Biol Chem 2000
:
Phosphorylated Tyr ( 1138 ) binds STAT3 to mediate its tyrosine phosphorylation and transcriptional activation, while phosphorylated
Tyr ( 985 ) binds the tyrosine phosphatase SHP-2 and reportedly
mediates both activation of ERK kinases and inhibition of LRb mediated
STAT3 activation
Schuringa et al., Oncogene 2001
(Cell Transformation, Neoplastic...) :
MEN2A-RET induces both
Tyr705 and Ser727 phosphorylation of STAT3, and
STAT3 serine phosphorylation is
required for its maximal transcriptional activity
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
Gao et al., J Immunol 2004
(Respiratory Distress Syndrome, Adult) :
Both
Tyr ( 705 ) and Ser ( 727 ) phosphorylation were
involved in
Stat3 activation as assessed in whole lung extracts
Jo et al., Life Sci 2004
(Translocation, Genetic) :
In this study, we observed that the stimulation of FPRL1 by
Trp-Lys-Tyr-Met-Val-D-Met ( WKYMVm )
caused serine phosphorylation but not tyrosine phosphorylation of
STAT3 in a pertussis toxin-sensitive manner
Lufei et al., Oncogene 2007
:
Transcriptional activity of
Stat3 is
controlled by
Tyr-phosphorylation , followed by dimerization and nuclear translocation
Jiang et al., J Biol Chem 2008
:
Tyr1138 in LEPRb was
required for leptin stimulated phosphorylation of
STAT3 but not JAK2 ( K882E )
Fu et al., PloS one 2012
(Carcinoma...) :
Results from co-immunoprecipitation and immunoblot analysis demonstrated that luteolin prevented the association between Hsp90 and
STAT3 and
induced both
Tyr ( 705 ) - and Ser ( 727 ) -phosphorylated STAT3 degradation through proteasome dependent pathway