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Identification of amino acid residues required for a specific interaction between Src‐tyrosine kinase and proline‐rich region of phosphatidylinositol‐3′ kinase
Author(s) -
Mak Paul,
He Zhiqing,
Kurosaki Tomohiro
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01179-9
Subject(s) - sh3 domain , proto oncogene tyrosine protein kinase src , tyrosine protein kinase csk , fyn , tyrosine kinase , biochemistry , kinase , phosphatidylinositol , sh2 domain , receptor tyrosine kinase , biology , mitogen activated protein kinase kinase , chemistry , microbiology and biotechnology , protein kinase a , signal transduction
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 Asp 92 , Tyr 93 , Arg 96 and Thr 97 of the SH3 domain of Fyn are essential for interacting with the proline‐rich peptide of PI‐3 kinase.