Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 32, Issue -, Pages 812-816Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0320812
Keywords
insulin resistance; insulin signalling; serine/threonine phosphorylation
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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.
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