Regulation of organelle membrane fusion by Pkc1p

被引：12

作者：

Lin, A

Patel, S

Latterich, M

机构：

[1] Salk Inst Biol Studies, La Jolla, CA 92037 USA

[2] Diversa Corp, San Diego, CA 92121 USA

来源：

TRAFFIC | 2001年 / 2卷 / 10期

关键词：

AAA protein; cdc48; membrane fusion; phosphorylation; protein kinase C; proteolysis; SNARE; Ubc7; ubiquitination; Ufe1;

D O I：

10.1034/j.1600-0854.2001.21004.x

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Membrane fusion relies on complex protein machineries, which act in sequence to catalyze the fusion of bilayers. The fusion of endoplasmic reticulum membranes requires the t-SNARE Ufe1p, and the AAA ATPase p97/Cdc48p. While the mechanisms of membrane fusion events have begun to emerge, little is known about how this fusion process is regulated. We provide first evidence that endoplasmic reticulum membrane fusion in yeast is regulated by the action of protein kinase G. Specifically, Pkc1p kinase activity is needed to protect the fusion machinery from ubiquitin-mediated degradation.

引用

收藏

页码：698 / 704

页数：7

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