Interaction of two proline-rich sequences of cell adhesion kinase β with SH3 domains of p130 Cas-related proteins and a GTPase-activating protein, Graf

被引：59

作者：

Ohba, T ^{[1
]}

Ishino, M ^{[1
]}

Aoto, H ^{[1
]}

Sasaki, T ^{[1
]}

机构：

[1] Sapporo Med Univ, Sch Med, Canc Res Inst, Dept Biochem,Chuo Ku, South 1,West 17, Sapporo, Hokkaido 060, Japan

来源：

BIOCHEMICAL JOURNAL | 1998年 / 330卷

关键词：

D O I：

10.1042/bj3301249

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cell adhesion kinase beta (CAK beta) is a protein tyrosine kinase closely related to focal adhesion kinase (FAK) in structure. CAK beta contains two proline-rich sequences within its C-terminal region. Since proline-rich sequences present in the corresponding region of FAK are known to mediate protein-protein interactions by binding to SH3 domains, we investigated binding of CAK beta to a panel of SH3 domains. Affinity precipitation from rat brain lysate revealed selective interactions of CAK beta with glutathione S-transferase (GST)-fused SH3 domains of p130(Cas)(Cas)-related proteins and Graf. Mutational analysis indicated that the proline-rich sequences of CAK beta mediate this interaction. Each of the two proline-rich sequences fused to GST bound directly to these SH3 domains in dot blot analysis. A competitive binding assay revealed that the first proline-rich sequence of CAK beta preferentially associated with the SH3 domain of Cas. The second proline-rich sequence of CAK beta bound to the SH3 domain of Graf with higher specificity than the corresponding proline-rich sequence of FAK. Finally, we showed co-immunoprecipitation of CAK beta with Graf from rat brain lysate. These results indicate that CAK beta associates in vivo with Graf through its SH3 domain.

引用

页码：1249 / 1254

页数：6

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