Identification of amino acid residues required for a specific interaction between Src‐tyrosine kinase and proline‐rich region of phosphatidylinositol‐3′ kinase

FEBS Letters

He, Zhiqing¹  Mak, Paul¹  Kurosaki, Tomohiro¹ 

[1] Wyeth-Ayerst Research, Molecular Biology Section, 401 N. Middletown Road, B205, Pearl River, NY 10965, USA

关键词: Fyn;    Phosphatidylinositol-3′ kinase;    Yeast;    two hybrid;    Site-directed mutagenesis;   

DOI  :  10.1016/S0014-5793(96)01179-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The binding of ligand to B-cell antigen receptors (BCR) leads to the activation of receptor-associated Src-family kinases and phosphatidylinositol-3′ kinase (PI-3 kinase). Although it has been demonstrated that SH3 domains of several Src-family kinases interact with PI-3 kinase by binding to a proline-rich region of PI-3 kinase in vitro, there is no direct evidence to support their interaction in vivo. Thus, we utilized the yeast two-hybrid assay to reconstitute this protein-protein interaction. This genetic screen clearly indicates that the interaction between SH3 domain of Fyn and the proline-rich region (residues: 80–104) of PI-3 kinase is highly specific. Mutational analysis revealed that amino acid residues Asp⁹², Tyr⁹³, Arg⁹⁶ and Thr⁹⁷ of the SH3 domain of Fyn are essential for interacting with the proline-rich peptide of PI-3 kinase.

【 授权许可】

Unknown