Premium
Insulin receptor substrate (IRS) transduction system: distinct and overlapping signaling potential
Author(s) -
Giovan Barbara,
Lucia Scaldaferri Maria,
Federici Massimo,
Porzio Ottavia,
Lauro Davide,
Fusco Angelo,
Sbraccia Paolo,
Borboni Patrizia,
Lauro Renato,
Sesti Giorgio
Publication year - 2000
Publication title -
diabetes/metabolism research and reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.307
H-Index - 110
eISSN - 1520-7560
pISSN - 1520-7552
DOI - 10.1002/1520-7560(2000)9999:9999<::aid-dmrr159>3.0.co;2-8
Subject(s) - insulin receptor , insulin receptor substrate , microbiology and biotechnology , sh2 domain , proto oncogene tyrosine protein kinase src , signal transduction , irs2 , irs1 , biology , tyrosine kinase , receptor , receptor tyrosine kinase , grb10 , insulin , biochemistry , chemistry , endocrinology , insulin resistance
Insulin receptor substrate (IRS) proteins play a central role in maintaining basic cellular functions such as growth and metabolism. They act as an interface between multiple growth factor receptors possessing tyrosine kinase activity, such as the insulin receptor, and a complex network of intracellular signalling molecules containing Src homology 2 (SH2) domains. Four members (IRS‐1, IRS‐2, IRS‐3, IRS‐4) of this family have been identified which differ in their subcellular distribution and interaction with SH2 domain proteins. In addition, differential IRS tissue‐ and developmental‐specific expression patterns may contribute to specificity in their signaling potential. Copyright © 2000 John Wiley & Sons, Ltd.