The p47 co‐factor regulates the ATPase activity of the membrane fusion protein, p97

FEBS Letters

Kondo, Hisao¹  Warren, Graham¹  Meyer, Hemmo H¹ 

[1] Cell Biology Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX, UK

关键词: p97;    p47;    AAA-ATPase;    Membrane fusion;    SNARE;    N-Ethylmaleimide-sensitive factor;    Soluble N-ethylmaleimide-sensitive factor attachment protein;   

DOI  :  10.1016/S0014-5793(98)01232-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The highly conserved ATPase p97, a member of the AAA-ATPases, is found in a complex with its co-factor p47 in rat liver cytosol. Previously it had been shown that p97-mediated reassembly of Golgi cisternae from mitotic Golgi fragments requires p47 which mediates the binding of p97 to a Golgi t-SNARE (soluble N-ethylmaleimide-sensitive factor attachment factor receptor), syntaxin 5. Here we show that it also suppresses the ATPase activity of p97 by up to 85% in a dose-dependent and saturable manner suggesting that it has other roles in the membrane fusion cycle.

【 授权许可】

Unknown