作者
Dominique Sawka-Verhelle, Sophie Tartare-Deckert, Morris F White, Emmanuel Van Obberghen
发表日期
1996/3/15
期刊
Journal of Biological Chemistry
卷号
271
期号
11
页码范围
5980-5983
出版商
Elsevier
简介
We compared the interaction between the insulin receptor (IR) and the IR substrate (IRS) proteins (IRS-1 and IRS-2) using the yeast two-hybrid system. Both IRS proteins interact specifically with the cytoplasmic portion of the IR and the related insulin-like growth factor-I receptor, and these interactions require receptor tyrosine kinase activity. Alignment of IRS-1 and IRS-2 revealed two conserved domains at the NH2 terminus, called IH1PH and IH2PTB, which resemble a pleckstrin homology (PH) domain and a phosphotyrosine binding (PTB) domain, respectively. The IH2PTB binds to the phosphorylated NPXY motif (Tyr-960) in the activated insulin receptor, providing a specific mechanism for the interaction between the receptor and IRS-1. Although the IH2PTB of IRS-2 also interacts with the NPEY motif of the insulin receptor, it is not essential for the interaction between the insulin receptor and IRS-2 in the yeast two …
引用总数
学术搜索中的文章
D Sawka-Verhelle, S Tartare-Deckert, MF White… - Journal of Biological Chemistry, 1996