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From signal transduction to signal interpretation: an alternative model for the molecular function of insulin receptor substrates


Boller, Simone; Joblin, Bradley A; Xu, Linhua; Item, Flurin; Trüb, Thomas; Boschetti, Nicola; Spinas, Giatgen A; Niessen, Markus (2012). From signal transduction to signal interpretation: an alternative model for the molecular function of insulin receptor substrates. Archives of Physiology and Biochemistry, 118(3):148-155.

Abstract

The insulin receptor (IR) recruits adaptor proteins, so-called insulin receptor substrates (IRS), to connect with downstream signalling pathways. A family of IRS proteins was defined based on three major common structural elements: Amino-terminal PH and PTB domains that mediate protein-lipid or protein-protein interactions, mostly carboxy-terminal multiple tyrosine residues that serve as binding sites for proteins that contain one or more SH2 domains and serine/threonine-rich regions which may be recognized by negative regulators of insulin action. The current model for the role of IRS proteins therefore combines an adaptor function with the integration of mostly negative input from other signal transduction cascades allowing for modulation of signalling amplitude. In this review we propose an extended version of the adaptor model that can explain how signalling specificity could be implemented at the level of IRS proteins.

Abstract

The insulin receptor (IR) recruits adaptor proteins, so-called insulin receptor substrates (IRS), to connect with downstream signalling pathways. A family of IRS proteins was defined based on three major common structural elements: Amino-terminal PH and PTB domains that mediate protein-lipid or protein-protein interactions, mostly carboxy-terminal multiple tyrosine residues that serve as binding sites for proteins that contain one or more SH2 domains and serine/threonine-rich regions which may be recognized by negative regulators of insulin action. The current model for the role of IRS proteins therefore combines an adaptor function with the integration of mostly negative input from other signal transduction cascades allowing for modulation of signalling amplitude. In this review we propose an extended version of the adaptor model that can explain how signalling specificity could be implemented at the level of IRS proteins.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Clinic for Endocrinology and Diabetology
Dewey Decimal Classification:610 Medicine & health
Language:English
Date:2012
Deposited On:25 Oct 2012 10:05
Last Modified:07 Dec 2017 15:41
Publisher:Informa Healthcare
ISSN:1381-3455
Free access at:PubMed ID. An embargo period may apply.
Publisher DOI:https://doi.org/10.3109/13813455.2012.671333
PubMed ID:22515179

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