Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose.

摘要: Abstract Insulin stimulates the autophosphorylation of tyrosine residues β subunit insulin receptor (IR); this modified insulin-independent kinase has increased activity toward exogenous substrates in vitro. We show here that replacement one or both twin tyrosines (residues 1162 and 1163) with phenylalanine results a dramatic reduction loss insulin-activated In vivo, these mutations not only result substantial decrease insulin-stimulated IR but also parallel uptake 2-deoxyglucose. Furthermore, truncated protein (lacking last 112 amino acids) an unstable subunit; mutant no vitro vivo does mediate is thus implicated regulation activities, 1163 as major sites regulation.