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INSR — JAK2

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: JAK2 → INSR (increases, JAK2 Activity) Gual et al., Endocrinology 1998*
  Evidence: Insulin and insulin-like growth factor-1 (IGF-1) treatment of cells overexpressing the insulin receptor or the IGF-1 receptor promotes phosphorylation and activation of Janus kinases JAK-1 and JAK-2

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: JAK2 — INSR (physical association, affinity chromatography technology) Le et al., Mol Endocrinol 2002*
• IRef Biogrid Interaction: JAK2 — INSR (physical association, affinity chromatography technology) Maegawa et al., Biochem Biophys Res Commun 1996*
• IRef Hprd Interaction: JAK2 — INSR (in vivo) Le et al., Mol Endocrinol 2002*

Text-mined interactions from Literome

Rocha et al., Curr Eye Res 2000 (Diabetes Mellitus, Experimental) : The activation of insulin receptors following insulin treatment, and the involvement of insulin receptor substrates-1 and -2, Shc, JAK-2 and STAT-1, were analyzed by immunoprecipitation, followed by SDS-PAGE and immunoblotting of rat lacrimal and salivary glands after exposure to insulin
Kellerer et al., Diabetologia 2001 (Hyperinsulinism...) : Furthermore, overexpression of the insulin receptor in HEK 293 cells clearly reduced JAK-2 phosphorylation and led further downstream to a diminished phosphatidylinositol 3-kinase activity
Ridderstråle et al., Endocrinology 1996 : Recent data suggest involvement of the Janus tyrosine kinase-2 (JAK2) in human GH-induced tyrosine phosphorylation of the GH receptor and the insulin receptor substrates 1 and 2 ( IRS-1 and IRS-2 ), leading to activation of the phosphatidylinositol 3-kinase and the acute insulin-like effects in primary rat adipocytes