Related Experiment Video
Updated: Aug 21, 2026

Studying the Hypothalamic Insulin Signal to Peripheral Glucose Intolerance with a Continuous Drug Infusion System into the Mouse Brain
Published on: January 4, 2018
Uncoupling insulin signalling by serine/threonine phosphorylation: a molecular basis for insulin resistance
1Department 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.
Related Concept Videos
Insulin: The Receptor and Signaling Pathways
Type II Diabetes II: Pathophysiology
PI3K/mTOR/AKT Signaling Pathway
Type II Diabetes I: Introduction
The JAK-STAT Signaling Pathway
Type I Diabetes II: Pathophysiology
