Gene interactions and pathways from curated databases and text-mining

◀ Back to STAT3

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