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Article

Decreased phosphorylation of mutant insulin receptor by protein kinase C and protein kinase A.

The Journal of biological chemistry - 30 Jun 1995

Miele C, Formisano P, Sohn K J, Caruso M, Pianese M, Palumbo G, Beguino L, Beguinot F

Abstract excerpt

We have recently reported that the Arg1152-->Gln insulin receptor mutation (QK single mutant) alters a conserved motif (RK motif) immediately next to the key tyrosine phosphorylation sites (Tyr1146, Tyr1150, Tyr1151) of the receptor and constitutively activates its kinase and metabolic signaling. To investigate further the function of the RK motif, we have expressed two additional mutant insulin receptors: a...

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PMID: 7797589
DOI: 10.1074/jbc.270.26.15844

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Decreased phosphorylation of mutant insulin receptor by protein kinase C and protein kinase A.PMID 7797589Read ↗

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Substitution of isoleucine for methionine at position 1153 in the beta-subunit of the human insulin receptor. A mutation that impairs receptor tyrosine kinase activity, receptor endocytosis, and insulin action.Semantic proximity Read ↗

Internalization of the constitutively active arginine 1152-->glutamine insulin receptor occurs independently of insulin at an accelerated rate.Semantic proximity Read ↗

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Functional characteristics of insulin receptors with a Thr-->Ser1200 mutation overexpressed in Chinese hamster ovary cells.Semantic proximity Read ↗

The regulatory role of known tyrosine autophosphorylation sites of the insulin receptor kinase domain. An assessment by replacement with neutral and negatively charged amino acids.Semantic proximity Read ↗

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