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*
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Summary
It is concluded that binding of hGrb10γ to IR decreases signaling through the IRS/PI 3-kinase/AKT pathway by physically blocking IRS access to IR.
- Type
- article
- Published
- 2003-03-07
- Cited by
- 117
- References
- 43
- Access
- Open access
- OpenAlex
- https://openalex.org/W1969744026
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:31026732
Keywords
Insulin receptor substrate, Insulin receptor, IRS1, IRS2, Phosphatidylinositol
References
- Insulin stimulates the kinase activity of RAC‐PK, a pleckstrin homology domain containing ser/thr kinase.
- Binding of SH2 containing proteins to the insulin receptor: A new way for modulating insulin signalling
- PTB Domains of IRS-1 and Shc Have Distinct but Overlapping Binding Specificities (*)
- The IRS-signalling system: A network of docking proteins that mediate insulin action
- The SH2/SH3 domain‐containing protein GRB2 interacts with tyrosine‐phosphorylated IRS1 and Shc: implications for insulin control of ras signalling.
- Grb10: A new substrate of the insulin-like growth factor I receptor.
- Grb10, a Positive, Stimulatory Signaling Adapter in Platelet-Derived Growth Factor BB-, Insulin-Like Growth Factor I-, and Insulin-Mediated Mitogenesis
- Characterization of an interaction between insulin receptor substrate 1 and the insulin receptor by using the two-hybrid system
- Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1
- Interaction between the Grb10 SH2 Domain and the Insulin Receptor Carboxyl Terminus (*)
- Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains.
- Interaction of a GRB-IR Splice Variant (a Human GRB10 Homolog) with the Insulin and Insulin-like Growth Factor I Receptors
- Identification of Grb10 as a direct substrate for members of the Src tyrosine kinase family
- Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B.
- Protein Kinase C-ζ Phosphorylates Insulin Receptor Substrate-1 and Impairs Its Ability to Activate Phosphatidylinositol 3-Kinase in Response to Insulin*
- Akt/Protein Kinase B Is Regulated by Autophosphorylation at the Hypothetical PDK-2 Site*
- Specific inhibition by hGRB10zeta of insulin-induced glycogen synthase activation: evidence for a novel signaling pathway.
- The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells.
- Grb-IR: a SH2-domain-containing protein that binds to the insulin receptor and inhibits its function.
- Insulin Receptor-mediated p62dok Tyrosine Phosphorylation at Residues 362 and 398 Plays Distinct Roles for Binding GTPase-activating Protein and Nck and Is Essential for Inhibiting Insulin-stimulated Activation of Ras and Akt*
Cited by
- Mitogenic roles of Gab1 and Grb10 as direct cellular partners in the regulation of MAP kinase signaling
- Investigating the role of the imprinted Grb10 gene in the regulation of maternal nutrient transfer.
- Protein kinase B (PKB/Akt), a key mediator of the PI3K signaling pathway.
- Dissecting the role and regulation of MRL function in Drosophila
- The Chemerin Receptor GPR1 Signals Through a RhoA/ROCK Pathway and Contributes to Glucose Homeostasis in Obese Mice
- Systemic Sclerosis is a Complex Disease Associated Mainly with Immune Regulatory and Inflammatory Genes
- Brain-Derived Neurotrophic Factor (BDNF) Modulation of Kv1.3 in the Olfactory Bulb
- On asymptotic properties of some complex Lorenz-like systems
- Cloning and transgenesis in mammals: Implications for xenotransplantation
- Placental expression of the insulin receptor binding protein GRB10: Relation to human fetoplacental growth and fetal gender.
- Insulin secretion and signaling in response to dietary restriction and subsequent re-alimentation in cattle.
- A disulfide-bond A oxidoreductase-like protein (DsbA-L) regulates adiponectin multimerization
- Growth Factor Receptor-binding Protein 10 (Grb10) as a Partner of Phosphatidylinositol 3-Kinase in Metabolic Insulin Action*
- GRB10 binds to LRP6, the Wnt co-receptor and inhibits canonical Wnt signaling pathway.
- Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2
- Grb-ing hold of insulin signaling
- The cell migration protein Grb7 associates with transcriptional regulator FHL2 in a Grb7 phosphorylation-dependent manner
- FLT3 signals via the adapter protein Grb10 and overexpression of Grb10 leads to aberrant cell proliferation in acute myeloid leukemia
- Tissue-specific regulation and function of Grb10 during growth and neuronal commitment
- Phosphorylation of Grb10 Regulates Its Interaction with 14-3-3*
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