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Updated: Aug 29, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening
Published on: August 29, 2015
Role of Ser/Thr kinases in the uncoupling of insulin signaling
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. It is associated with the development of type II diabetes, a 21st century epidemic. 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 cardinal role of Ser/Thr protein kinases, which phosphorylate insulin receptor substrates, as key players in the uncoupling of insulin signaling and the induction of an insulin resistance state.
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Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
