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Biochem Soc Trans. 2004 Nov;32(Pt 5):812-6.

Uncoupling insulin signalling by serine/threonine phosphorylation: a molecular basis for insulin resistance.

Author information

1
Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot 76100, Israel. yehiel.zick@weizmann.ac.il

Abstract

Insulin resistance refers to a decreased capacity of circulating insulin to regulate nutrient metabolism. Recent studies reveal that agents that induce insulin resistance exploit phosphorylation-based negative feedback control mechanisms otherwise utilized by insulin itself to uncouple the insulin receptor from its downstream effectors and thereby terminate insulin signal transduction. This article focuses on the Ser/Thr protein kinases which phosphorylate insulin receptor substrates and the major Ser sites that are phosphorylated, as key elements in the uncoupling of insulin signalling and the induction of an insulin resistance state.

PMID:
15494022
DOI:
10.1042/BST0320812
[Indexed for MEDLINE]

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