Gene interactions and pathways from curated databases and text-mining

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IGF1 — TYR

Text-mined interactions from Literome

Byun et al., J Endocrinol 2001 : The IGF-I binding activity was also dramatically reduced by the mutation Cys18/Tyr , and to a lesser extent, by the mutation Cys17/Ser or Cys20/Ser
Leahy et al., J Biol Chem 2004 (Lymphoma, B-Cell...) : Although phosphorylation of Gab2 was similar in WT and mutant cell lines, phosphorylation of Shc on Tyr ( 313 ) in response to IGF-I was decreased in cells expressing the mutant receptor, as was recruitment of Grb2 and Ship to Shc
Harwood et al., J Biol Chem 2008 (MAP Kinase Signaling System) : In Rh1 cells rapamycin inhibited insulin-like growth factor-I (IGF-I) stimulated phosphorylation of Thr ( 202 ) but not Tyr ( 204 ) and suppressed activation of p44/42 kinase activity ... Down-regulation of raptor, which inhibits mTORC1 signaling, had a similar effect to rapamycin in blocking IGF-I stimulated Tyr ( 204 ) phosphorylation
Nemoto et al., Neuropharmacology 2010 : In SB216763 treated cells, IGF-I induced Tyr-autophosphorylation of IGF-I receptor was decreased by 36 %, compared to nontreated cells
Shen et al., Cell Mol Life Sci 2010 (MAP Kinase Signaling System) : Pyk2 recruitment to SHPS-1 is mediated via the interaction of Pyk2 Tyr402 and the Src in response to IGF-I
Bayne et al., J Biol Chem 1990 : Thus, Tyr24 , Tyr31, and Tyr60 are involved in the high affinity binding of IGF-I to the type 1 IGF receptor, while Tyr60 is important for maintaining binding to the type 2 IGF receptor
Crossland et al., Am J Physiol Endocrinol Metab 2013 : These blunted responses were associated with attenuated IGF-I induced FAK Tyr ( 397 ) phosphorylation and markedly suppressed phosphorylation of tuberous sclerosis complex 2 (TSC2) and critical downstream mTOR signaling ( ribosomal S6 kinase, eIF4F assembly ) in FAK shRNA cells ( all P < 0.05 vs. IGF-I treated SCR cells )
Shemer et al., J Biol Chem 1987 : Tyrosine kinase activity of the IGF-I receptors was demonstrated by IGF-I induced phosphorylation of the exogenous substrate poly ( Glu, Tyr ) 4 : 1 in both cell types