Scholay

学术搜索 · AI 审稿 · LaTeX 协作

An Alternative to SH2 Domains for Binding Tyrosine-Phosphorylated Proteins

作者:W. Michael Kavanaugh, Lewis T. Williams · 发表于:Science · 年份:1994 · DOI:10.1126/science.7527937 · 被引用次数:508 · 研究领域:Protein Kinase Regulation and GTPase Signaling、PI3K/AKT/mTOR signaling in cancer、Cell Adhesion Molecules Research

Src homology 2 (SH2) domains bind specifically to tyrosine-phosphorylated proteins that participate in signaling by growth factors and oncogenes. A protein domain was identified that bound specifically to the tyrosine-phosphorylated form of its target protein but differs from known SH2 sequences. Phosphotyrosine-binding (PTB) domains were found in two proteins: SHC, a protein implicated in signaling through Ras; and SCK, encoded by a previously uncharacterized gene. The PTB domain of SHC specifically bound to a tyrosine-phosphorylated 145-kilodalton protein. PTB domains are an alternative to SH2 domains for specifically recruiting tyrosine-phosphorylated proteins into signaling complexes and are likely to take part in signaling by many growth factors.