Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
about
SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinaseHuman GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domainsThe adapter protein ZIP binds Grb14 and regulates its inhibitory action on insulin signaling by recruiting protein kinase CzetaGrb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesisTwo adaptor proteins differentially modulate the phosphorylation and biophysics of Kv1.3 ion channel by SRC kinaseThe Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptorRegulation of insulin and type 1 insulin-like growth factor signaling and action by the Grb10/14 and SH2B1/B2 adaptor proteinsStructural basis for dimerization of the Grb10 Src homology 2 domain. Implications for ligand specificityGrb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferationAssociation of fibroblast growth factor receptor 1 with the adaptor protein Grb14. Characterization of a new receptor binding partnerIdentification of Grb10 as a direct substrate for members of the Src tyrosine kinase familyEvidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2The Grb7 family proteins: structure, interactions with other signaling molecules and potential cellular functionsInteraction of MAD2 with the carboxyl terminus of the insulin receptor but not with the IGFIR. Evidence for release from the insulin receptor after activationTwo novel proteins that are linked to insulin-like growth factor (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signalingmGrb10 interacts with Nedd4Identification of the rat adapter Grb14 as an inhibitor of insulin actionsThe adapter protein Grb10 associates preferentially with the insulin receptor as compared with the IGF-I receptor in mouse fibroblastsThe PIR domain of Grb14 is an intrinsically unstructured protein: implication in insulin signalingDisruption of a putative SH3 domain and the proline-rich motifs in the 53-kDa substrate of the insulin receptor kinase does not alter its subcellular localization or ability to serve as a substrate.Four PSM/SH2-B alternative splice variants and their differential roles in mitogenesis.Inhibition of hGrb10 binding to the insulin receptor by functional domain-mediated oligomerization.Inhibition of insulin receptor catalytic activity by the molecular adapter Grb14.Ligand-mediated endocytosis and trafficking of the insulin-like growth factor receptor I and insulin receptor modulate receptor function.Carrageenan Inhibits Insulin Signaling through GRB10-mediated Decrease in Tyr(P)-IRS1 and through Inflammation-induced Increase in Ser(P)307-IRS1Insulin and insulin-like growth factor II differentially regulate endocytic sorting and stability of insulin receptor isoform AGrb10 and Grb14: enigmatic regulators of insulin action--and more?DNA methylation at differentially methylated regions of imprinted genes is resistant to developmental programming by maternal nutrition.Analysis of a peptide hormone-receptor interaction in the yeast two-hybrid system.Abnormalities of IGF-I signaling in the pathogenesis of diseases of the bone, brain, and fetoplacental unit in humans.Inputs and outputs of insulin receptor.Grb10 is a dual regulator of receptor tyrosine kinase signaling.Grb10 inhibits insulin-stimulated insulin receptor substrate (IRS)-phosphatidylinositol 3-kinase/Akt signaling pathway by disrupting the association of IRS-1/IRS-2 with the insulin receptor.FLT3 signals via the adapter protein Grb10 and overexpression of Grb10 leads to aberrant cell proliferation in acute myeloid leukemiaGrowth factor receptor-binding protein 10 (Grb10) as a partner of phosphatidylinositol 3-kinase in metabolic insulin action.Reduced cell attachment and phosphorylation of focal adhesion kinase associated with expression of a mutant insulin receptor.Structure and function of the insulin-like growth factor I receptor.APS, an adapter protein with a PH and SH2 domain, is a substrate for the insulin receptor kinase.The BPS domain of Grb10 inhibits the catalytic activity of the insulin and IGF1 receptors.Inhibition of FGF receptor signalling in Xenopus oocytes: differential effect of Grb7, Grb10 and Grb14.
P2860
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P2860
Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
description
1996 nî lūn-bûn
@nan
1996 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
@ast
Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
@en
Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
@nl
type
label
Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
@ast
Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
@en
Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
@nl
prefLabel
Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
@ast
Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
@en
Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
@nl
P2093
P921
P356
P1476
Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus
@en
P2093
U Svensson
P304
P356
10.1074/JBC.271.15.8882
P407
P577
1996-04-12T00:00:00Z