The insulin signalling system and the IRS proteins
MF White - Diabetologia, 1997 - Springer
Diabetologia, 1997•Springer
During the past few years, the insulin signalling system has emerged as a flexible network of
interacting proteins. By utilizing the insulin receptor substrate (IRS)-proteins (IRS-1 and IRS-
2), the insulin signal can be amplified or attenuated independently of insulin binding and
tyrosine kinase activity, providing an extensible mechanism for signal transmission in
multiple cellular backgrounds. By employing IRS-proteins to engage various signalling
proteins, the insulin receptor avoids the stoichiometric constraints encountered by receptors …
interacting proteins. By utilizing the insulin receptor substrate (IRS)-proteins (IRS-1 and IRS-
2), the insulin signal can be amplified or attenuated independently of insulin binding and
tyrosine kinase activity, providing an extensible mechanism for signal transmission in
multiple cellular backgrounds. By employing IRS-proteins to engage various signalling
proteins, the insulin receptor avoids the stoichiometric constraints encountered by receptors …
Summary
During the past few years, the insulin signalling system has emerged as a flexible network of interacting proteins. By utilizing the insulin receptor substrate (IRS)-proteins (IRS-1 and IRS-2), the insulin signal can be amplified or attenuated independently of insulin binding and tyrosine kinase activity, providing an extensible mechanism for signal transmission in multiple cellular backgrounds. By employing IRS-proteins to engage various signalling proteins, the insulin receptor avoids the stoichiometric constraints encountered by receptors which directly recruit SH2-proteins to their autophosphorylation sites. Finally, the shared use of IRS-proteins by multiple receptors is likely to reveal important connections between insulin and other hormones and cytokines which were previously unrecognized, or observed but unexplained. [Diabetologia (1997) 40: S 2–S 17]
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