IRS2

From Wikipedia, the free encyclopedia

Insulin receptor substrate 2

Identifiers

External IDs

OMIM: 600797 MGI: 109334 HomoloGene: 2778

Gene ontology
Molecular Function:	• signal transducer activity • insulin receptor binding • protein binding • protein kinase binding
Biological Process:	• glucose metabolic process • signal transduction • brain development • cell proliferation • positive regulation of cell proliferation • insulin receptor signaling pathway

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003749 (mRNA)
NP_003740 (protein)

XM_357863 (mRNA)
XP_357863 (protein)

Location

Chr 13: 109.2 - 109.24 Mb

Chr 8: 11 - 11.01 Mb

Pubmed search

[1]

[2]

Insulin receptor substrate 2, also known as IRS2, is a human gene.

This gene encodes the insulin receptor substrate 2, a cytoplasmic signaling molecule that mediates effects of insulin, insulin-like growth factor 1, and other cytokines by acting as a molecular adaptor between diverse receptor tyrosine kinases and downstream effectors. The product of this gene is phosphorylated by the insulin receptor tyrosine kinase upon receptor stimulation, as well as by an interleukin 4 receptor-associated kinase in response to IL4 treatment.^[1]. Mice lacking IRS2 have a diabetic phenotype as well as a 40% reduction in brain mass.

[edit] References

^ Entrez Gene: IRS2 insulin receptor substrate 2.

[edit] Further reading

White MF (1999). "The IRS-signalling system: a network of docking proteins that mediate insulin action.". Mol. Cell. Biochem. 182 (1-2): 3–11. PMID 9609109.
Jiang H, Harris MB, Rothman P (2000). "IL-4/IL-13 signaling beyond JAK/STAT.". J. Allergy Clin. Immunol. 105 (6 Pt 1): 1063–70. PMID 10856136.
Sesti G, Federici M, Hribal ML, et al. (2001). "Defects of the insulin receptor substrate (IRS) system in human metabolic disorders.". FASEB J. 15 (12): 2099–111. doi:10.1096/fj.01-0009rev. PMID 11641236.
Gibson SL, Ma Z, Shaw LM (2007). "Divergent roles for IRS-1 and IRS-2 in breast cancer metastasis.". Cell Cycle 6 (6): 631–7. PMID 17361103.
Dearth RK, Cui X, Kim HJ, et al. (2007). "Oncogenic transformation by the signaling adaptor proteins insulin receptor substrate (IRS)-1 and IRS-2.". Cell Cycle 6 (6): 705–13. PMID 17374994.
Johnston JA, Wang LM, Hanson EP, et al. (1996). "Interleukins 2, 4, 7, and 15 stimulate tyrosine phosphorylation of insulin receptor substrates 1 and 2 in T cells. Potential role of JAK kinases.". J. Biol. Chem. 270 (48): 28527–30. PMID 7499365.
Patti ME, Sun XJ, Bruening JC, et al. (1995). "4PS/insulin receptor substrate (IRS)-2 is the alternative substrate of the insulin receptor in IRS-1-deficient mice.". J. Biol. Chem. 270 (42): 24670–3. PMID 7559579.
Sun XJ, Wang LM, Zhang Y, et al. (1995). "Role of IRS-2 in insulin and cytokine signalling.". Nature 377 (6545): 173–7. doi:10.1038/377173a0. PMID 7675087.
Ridderstråle M, Degerman E, Tornqvist H (1995). "Growth hormone stimulates the tyrosine phosphorylation of the insulin receptor substrate-1 and its association with phosphatidylinositol 3-kinase in primary adipocytes.". J. Biol. Chem. 270 (8): 3471–4. PMID 7876077.
Platanias LC, Uddin S, Yetter A, et al. (1996). "The type I interferon receptor mediates tyrosine phosphorylation of insulin receptor substrate 2.". J. Biol. Chem. 271 (1): 278–82. PMID 8550573.
Beitner-Johnson D, Blakesley VA, Shen-Orr Z, et al. (1996). "The proto-oncogene product c-Crk associates with insulin receptor substrate-1 and 4PS. Modulation by insulin growth factor-I (IGF) and enhanced IGF-I signaling.". J. Biol. Chem. 271 (16): 9287–90. PMID 8621590.
Sawka-Verhelle D, Tartare-Deckert S, White MF, Van Obberghen E (1996). "Insulin receptor substrate-2 binds to the insulin receptor through its phosphotyrosine-binding domain and through a newly identified domain comprising amino acids 591-786.". J. Biol. Chem. 271 (11): 5980–3. PMID 8626379.
He W, Craparo A, Zhu Y, et al. (1996). "Interaction of insulin receptor substrate-2 (IRS-2) with the insulin and insulin-like growth factor I receptors. Evidence for two distinct phosphotyrosine-dependent interaction domains within IRS-2.". J. Biol. Chem. 271 (20): 11641–5. PMID 8662806.
Zhang WR, Li PM, Oswald MA, Goldstein BJ (1996). "Modulation of insulin signal transduction by eutopic overexpression of the receptor-type protein-tyrosine phosphatase LAR.". Mol. Endocrinol. 10 (5): 575–84. PMID 8732688.
Argetsinger LS, Norstedt G, Billestrup N, et al. (1997). "Growth hormone, interferon-gamma, and leukemia inhibitory factor utilize insulin receptor substrate-2 in intracellular signaling.". J. Biol. Chem. 271 (46): 29415–21. PMID 8910607.
Thiselton DL, Hampson RM, Nayudu M, et al. (1997). "Mapping the RP2 locus for X-linked retinitis pigmentosa on proximal Xp: a genetically defined 5-cM critical region and exclusion of candidate genes by physical mapping.". Genome Res. 6 (11): 1093–102. PMID 8938433.
Izuhara K, Harada N (1997). "Interleukin-4 activates two distinct pathways of phosphatidylinositol-3 kinase in the same cells.". Biochem. Biophys. Res. Commun. 229 (2): 624–9. doi:10.1006/bbrc.1996.1854. PMID 8954948.
Vanhaesebroeck B, Welham MJ, Kotani K, et al. (1997). "P110delta, a novel phosphoinositide 3-kinase in leukocytes.". Proc. Natl. Acad. Sci. U.S.A. 94 (9): 4330–5. PMID 9113989.
Sawka-Verhelle D, Baron V, Mothe I, et al. (1997). "Tyr624 and Tyr628 in insulin receptor substrate-2 mediate its association with the insulin receptor.". J. Biol. Chem. 272 (26): 16414–20. PMID 9195949.
Algenstaedt P, Antonetti DA, Yaffe MB, Kahn CR (1997). "Insulin receptor substrate proteins create a link between the tyrosine phosphorylation cascade and the Ca2+-ATPases in muscle and heart.". J. Biol. Chem. 272 (38): 23696–702. PMID 9295312.