期刊
TRAFFIC
卷 11, 期 4, 页码 468-478出版社
WILEY
DOI: 10.1111/j.1600-0854.2010.01034.x
关键词
Atg18; myotubularins; phosphoinositides; PtdIns3P phosphatase; WIPI-1 alpha
类别
资金
- Special Coordination Funds for Promoting Science, Technology of the Ministry of Education, Culture, Sports, Science and Technology (MEXT)
- Japan Society for the Promotion of Science (JSPS)
- BBSRC [BB/H000631/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H000631/1, BBS/E/B/00001221] Funding Source: researchfish
Autophagy is a catabolic process that delivers cytoplasmic material to the lysosome for degradation. The mechanisms regulating autophagosome formation and size remain unclear. Here, we show that autophagosome formation was triggered by the overexpression of a dominant-negative inactive mutant of Myotubularin-related phosphatase 3 (MTMR3). Mutant MTMR3 partially localized to autophagosomes, and PtdIns3P and two autophagy-related PtdIns3P-binding proteins, GFP-DFCP1 and GFP-WIPI-1 alpha (WIPI49/Atg18), accumulated at sites of autophagosome formation. Knock-down of MTMR3 increased autophagosome formation, and overexpression of wild-type MTMR3 led to significantly smaller nascent autophagosomes and a net reduction in autophagic activity. These results indicate that autophagy initiation depends on the balance between PI 3-kinase and PI 3-phosphatase activity. Local levels of PtdIns3P at the site of autophagosome formation determine autophagy initiation and the size of the autophagosome membrane structure.
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