Dephosphorylation of clustered phosphoserine residues in human Grb14 by protein phosphatase 1 and its effect on insulin receptor complex formation
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Summary
Phosphatase‐mediated dephosphorylation of the hGrb14 phosphoserine residues is investigated, and it is suggested that phosphate groups on Ser358 and Ser362 in h Grb14 are de phosphorylated by PP1, and the deph phosphorylation facilitates hGrB14–IR complex formation.
- Type
- article
- Published
- 2019-07-25
- Cited by
- 1
- References
- 29
- OpenAlex
- https://openalex.org/W2965604214
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:198911913
Keywords
Phosphoserine, Dephosphorylation, Chemistry, Insulin receptor, DUSP6
References
- Fine Mapping and Candidate Gene Search of Quantitative Trait Loci for Growth and Obesity Using Mouse Intersubspecific Subcongenic Intercrosses and Exome Sequencing
- Genetic polymorphisms associated with overweight and obesity in uncontrolled Type 2 diabetes mellitus.
- Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase.
- Multiple phosphorylation of rabbit skeletal muscle glycogen synthase. Evidence for interactions among phosphorylation sites and the resolution of electrophoretically distinct forms of the subunit.
- Identifying Candidate Genes for Type 2 Diabetes Mellitus and Obesity through Gene Expression Profiling in Multiple Tissues or Cells
- 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*
- Improved glucose homeostasis and enhanced insulin signalling in Grb14‐deficient mice
- Identification of New Hub Genes Associated with Bladder Carcinoma via Bioinformatics Analysis
- Regulation of protein phosphatase-1.
- Grb10 and Grb14: enigmatic regulators of insulin action--and more?
- Identification of the Rat Adapter Grb14 as an Inhibitor of Insulin Actions*
- Regulation of insulin and type 1 insulin‐like growth factor signaling and action by the Grb10/14 and SH2B1/B2 adaptor proteins
- The BPS domain of Grb10 inhibits the catalytic activity of the insulin and IGF1 receptors
- Grb10 Interacts Differentially with the Insulin Receptor, Insulin-like Growth Factor I Receptor, and Epidermal Growth Factor Receptor via the Grb10 Src Homology 2 (SH2) Domain and a Second Novel Domain Located between the Pleckstrin Homology and SH2 Domains*
- Structural basis for inhibition of the insulin receptor by the adaptor protein Grb14.
- A novel CDK5‐dependent pathway for regulating GSK3 activity and kinesin‐driven motility in neurons
- Reconstitution of a Mg‐ATP‐dependent protein phosphatase and its activation through a phosphorylation mechanism
- Genetic Effects on Longitudinal Changes from Healthy to Adverse Weight and Metabolic Status — The HUNT Study
- Inhibition of Insulin Receptor Catalytic Activity by the Molecular Adapter Grb14*
- Phosphorylation of Grb14 BPS domain by GSK-3 correlates with complex forming of Grb14 and insulin receptor.
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