川崎医科大学 教員情報   
     


  クリバヤシ フトシ   Futoshi Kuribayashi
  栗林 太
   所属   川崎医科大学  医学部 基礎医学 生化学
   職種   教授
論文種別 原著
単著/共著の別 共著
言語種別 英語
査読の有無 査読あり
表題 A region C-terminal to the Proline-rich Core of p47phox regulates Activation of the Phagocyte NADPH oxidase by Interacting with the C-terminal SH3 Domain of p67phox.
掲載誌名 正式名:Archives of Biochemistry and Biophysics
略  称:Arch. Biochem. Biophys
巻・号・頁 444(2),185-194頁
著者・共著者 Mizuki Kazuhito, Takeya Ryu, Kuribayashi Futoshi, Nobuhisa Ikuo, Kohda Daisuke, Nunoi Hiroyuki, Takeshige Koichiro, Sumimoto Hideki.
発行年月 2005/12
概要 Activation of the phagocyte NADPH oxidase requires the regulatory proteins p47phox and p67phox, each harboring two SH3 domains. p67phox interacts with p47phox via simultaneous binding of the p67phox C-terminal SH3 domain to both the proline-rich region (PRR) of amino acid residues 360-369 and its C-terminally flanking region of p47phox; the role of the interaction in oxidase regulation has not been fully understood. Here we show that the p47phox-p67phox interaction is disrupted not only by deletion of the PRR but also by substitution for basic residues in the extra-PRR (K383E/K385E). The substitution impaired oxidase activation partially in vitro and much more profoundly in vivo, indicating the significance of the p47phox extra-PRR. Replacement of Ser-379 in the extra-PRR, a residue known to undergo phosphorylation in stimulated cells, by aspartate attenuates the interaction and thus results in a defective superoxide production, suggesting that phosphorylation of Ser-379 is involved in oxidase regulation.