The IRS-signalling system: a network of docking proteins that mediate insulin action (Q28272481)

Molecular and Cellular Biochemistry

Europe PubMed Central

title

The IRS-signalling system: a network of docking proteins that mediate insulin action (English)

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M F White

1

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language of work or name

English

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publication date

May 1998

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published in

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volume

182

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page(s)

3-11

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issue

1-2

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cites work

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Interleukin 1 (IL1) and tumour necrosis factor (TNF) signal transduction

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Alternative pathway of insulin signalling in mice with targeted disruption of the IRS-1 gene.

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Association of insulin receptor substrate-1 with integrins

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Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor

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Protein modules and signalling networks

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The Fyn tyrosine kinase binds Irs-1 and forms a distinct signaling complex during insulin stimulation

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Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok

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Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras

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Regulation of neuronal survival by the serine-threonine protein kinase Akt

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IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha- and obesity-induced insulin resistance

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Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1.

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Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling.

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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

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Development of a novel polygenic model of NIDDM in mice heterozygous for IR and IRS-1 null alleles

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Adapter function of protein-tyrosine phosphatase 1D in insulin receptor/insulin receptor substrate-1 interaction

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The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signalling

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Neurite outgrowth of PC12 cells is suppressed by wortmannin, a specific inhibitor of phosphatidylinositol 3-kinase

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Cloning of the mouse insulin receptor substrate-1 (IRS-1) gene and complete sequence of mouse IRS-1.

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Akt signaling: linking membrane events to life and death decisions

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14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner

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Regulation of phosphatidylinositol 3'-kinase by tyrosyl phosphoproteins. Full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit

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Activation of protein kinase C (alpha, beta, and zeta) by insulin in 3T3/L1 cells. Transfection studies suggest a role for PKC-zeta in glucose transport

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The IRS-2 gene on murine chromosome 8 encodes a unique signaling adapter for insulin and cytokine action.

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Structural organization and alternative splicing of the murine phosphoinositide 3-kinase p85 alpha gene

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Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells

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Regulation of chemotaxis by the platelet-derived growth factor receptor-beta

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Insulin-stimulated phosphatidylinositol 3-kinase. Association with a 185-kDa tyrosine-phosphorylated protein (IRS-1) and localization in a low density membrane vesicle

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The ubiquitously expressed Syp phosphatase interacts with c-kit and Grb2 in hematopoietic cells

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Role of IRS-2 in insulin and cytokine signalling

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The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp

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Role of IRS-1-GRB-2 complexes in insulin signaling

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The 60 kDa insulin receptor substrate functions like an IRS protein (pp60IRS3) in adipose cells

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Tyrosyl phosphorylation and growth factor receptor association of the human corkscrew homologue, SH-PTP2.

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Mouse and human SHPS-1: molecular cloning of cDNAs and chromosomal localization of genes

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Insulin stimulation of phosphatidylinositol 3-kinase activity maps to insulin receptor regions required for endogenous substrate phosphorylation

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Increased adipose tissue expression of tumor necrosis factor-alpha in human obesity and insulin resistance

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