Deletion of the insulin receptor beta-subunit acidic domain results in enhanced metabolic signaling.
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Summary
The observed changes in biological signaling indicate that specific pathways diverge at the level of the receptor itself and that neither kinase activity or biological activity necessarily correlates directly with diminished autophosphorylation when the tyrosine kinase domain remains intact.
- Type
- article
- Published
- 1993-09-01
- Cited by
- 2
- References
- 26
- OpenAlex
- https://openalex.org/W2040621819
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:41744133
Keywords
Autophosphorylation, Insulin receptor, IRS2, Insulin receptor substrate, Biology
References
- Metabolism and growth
- Mutation of the two carboxyl-terminal tyrosines results in an insulin receptor with normal metabolic signaling but enhanced mitogenic signaling properties.
- Tyrosine phosphorylation of the insulin receptor beta subunit activates the receptor-associated tyrosine kinase activity.
- Amino acid sequences Gly-Pro-Leu-Tyr and Asn-Pro-Glu-Tyr in the submembranous domain of the insulin receptor are required for normal endocytosis.
- Characterization of an insulin receptor mutant lacking the subunit processing site.
- An endogenous substrate for the insulin receptor-associated tyrosine kinase.
- The role of insulin receptor kinase domain autophosphorylation in receptor-mediated activities. Analysis with insulin and anti-receptor antibodies.
- Augmented mitogenesis and impaired metabolic signaling mediated by a truncated insulin receptor.
- Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor.
- Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells
- Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes
- Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free system
- After insulin binds.
- The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.
- In vitro tyrosine phosphorylation studies on RAS proteins and calmodulin suggest that polylysine-like basic peptides or domains may be involved in interactions between insulin receptor kinase and its substrate.
- Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose.
- The NPEY sequence is not necessary for endocytosis and processing of insulin-receptor complexes.
- Defective insulin receptor function in down-regulated HepG2 cells.
- Insulin rapidly stimulates phosphorylation of a 46-kDa membrane protein on tyrosine residues as well as phosphorylation of several soluble proteins in intact fat cells.
- Basic polycations activate the insulin receptor kinase and a tightly associated serine kinase.
Cited by
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- Transmembrane signalling by insulin via an insulin receptor mutated at tyrosines 1158, 1162, and 1163.
- The purified COOH-terminal domain of the insulin receptor carries activity to stimulate protein kinase activity or autophosphorylation of the beta subunit domain of insulin receptor.
- Insulin-receptor autophosphorylation and kinase activity are constitutively increased in fibroblasts cultured from a patient with heritable insulin-resistance.