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

被引：89

作者：

Meyer, HH ^{[1
]}

Kondo, H ^{[1
]}

Warren, G ^{[1
]}

机构：

[1] Imperial Canc Res Fund, Cell Biol Lab, London WC2A 3PX, England

来源：

FEBS LETTERS | 1998年 / 437卷 / 03期

关键词：

p97; p47; AAA-ATPase; membrane fusion; SNARE; N-ethylmaleimide-sensitive factor; soluble N-ethylmaleimide-sensitive factor attachment protein;

D O I：

10.1016/S0014-5793(98)01232-0

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：

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. (C) 1998 Federation of European Biochemical Societies.

引用

页码：255 / 257

页数：3

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