期刊
FEBS LETTERS
卷 580, 期 19, 页码 4632-4638出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2006.07.041
关键词
Cvt pathway; proaminopeptidase I; autophagy; phosphatidylinositolphosphate; lipid binding; FRRGT motif
Atg18 and Atg21 are homologous S. cerevisiae autophagy proteins. Atg18 is essential for biogenesis of Cvt vesicles and autophagosomes, while Atg21 is only essential for Cvt vesicle formation. We found that mutated Atg18-(FTTGT), which lost almost completely its binding to PtdIns3P and PtdIns(3,5)P-2, is non-functional during the Cvt pathway but active during autophagy and pexophagy. Since the Cvt pathway does not depend on PtdIns(3,5)P-2, we conclude that the Cvt pathway requires binding of Atg18 to PtdIns3P. Mutated Atg21-(FTTGT) is inactive during the Cvt pathway but showed only partly reduced binding to PtdIns-phosphates, suggesting further lipid binding domains in Atg21. GFP-Atg18-(FTTGT) and Atg21-(FTTGT)-GFP are released from vacuolar punctae to the cytosol. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据