An SH3 domain‐mediated interaction between the phagocyte NADPH oxidase factors p40 phoxand p47 phox

FEBS Letters

Sumimoto, Hideki¹  Ito, Takashi²  Sakaki, Yoshiyuki²  Takeshige, Koichiro¹  Nakamura, Rika² 

[1] Department of Biochemistry, Kyushu University School of Medicine, Higashi-ku, Fukuoka 812, Japan;Human Genome Center, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108, Japan

关键词: NADPH oxidase;    SH3 domain;    Proline-rich region;    CGD;    chronic granulomatous disease;    SH3;    Src homology 3;    GST;    glutathione S-transferase;    MBP;    maltose binding protein;   

DOI  :  10.1016/0014-5793(96)00387-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The phagocyte NADPH oxidase is activated during phagocytosis to produce superoxide, following assembly of a membrane-integrated cytochrome b ₅₅₈ with cytosolic proteins, p47 ^phox , p67 ^phox and p40 ^phox, each containing Src homology 3 (SH3) domains. While both p47 ^phox and p67 ^phox are indispensable for the oxidase activity, role of p40 ^phox remains obscure. Here we study interaction between p40 ^phox and p47 ^phox by two independent methods, a two-hybrid system in the yeast and an in vitro binding assay using purified proteins. The present results show that the interaction is mediated via binding of the SH3 domain of p40 ^phox to a C-terminal proline-rich region of p47 ^phox . This proline-rich region is also the target for binding of p67 ^phox , and the SH3 domain of p40 ^phox can inhibit the binding of the C-terminal one of p67 ^phox to p47 ^phox .

【 授权许可】

Unknown