Reconstitution of GTP‐γ‐S‐dependent phospholipase D activity with ARF, RhoA, and a soluble 36‐kDa protein

FEBS Letters

Nakamura, Shun-ichi¹  Hitomi, Tomohiro¹  Yoshida, Kimihisa¹  Jinnai, Hitoshi¹  Ogino, Chiaki²  Akisue, Toshihiro¹  Nishizuka, Yasutomi¹  Shimooku, Kiyoshi¹ 

[1]Department of Biochemistry, Kobe University School of Medicine, Kobe 650, Japan

关键词: Phospholipase D;    ADP-ribosylation factor;    RhoA;    G-protein;    PLD;    phospholipase D;    PtdCho;    phosphatidylcholine;    G-protein;    GTP-binding regulatory protein;    ARF;    ADP-ribosylation factor;    GTP-γ-S;    guanosine 5′-O-(3-thiotriphosphate);    PtdEtn;    phosphatidylethanolamine;    PtdEtOH;    phosphatidylethanol;    PKC;    protein kinase C;   

DOI  :  10.1016/0014-5793(96)00483-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

For activation of kidney membrane phospholipase D (PLD), cytosol is absolutely needed in addition to GTP-γ-S. The active component of cytosol consists of three protein factors: ADP-ribosylation factor, RhoA, and a soluble 36-kDa protein. Any combination of these two factors synergistically activates PLD to some extent, but the presence of the three factors causes full activation. The 36-kDa protein is stable at 60°C but inactivated at 80°C for 10 min. Tissue distribution of the 36-kDa protein roughly coincides with that of PLD, suggesting physiological relevance of the protein in the regulation of PLD.

【 授权许可】

Unknown