期刊
JOURNAL OF CELL BIOLOGY
卷 182, 期 4, 页码 685-701出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200803137
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资金
- Biotechnology and Biological Sciences Research Council (BBSRC)
- BBSRC special committee studentship
- Biotechnology and Biological Sciences Research Council [BBS/E/B/00001116, BBS/E/B/0000C116] Funding Source: researchfish
Autophagy is the engulfment of cytosol and organelles by double-membrane vesicles termed autophagosomes. Autophagosome formation is known to require phosphatidylinositol 3-phosphate (PI(3) P) and occurs near the endoplasmic reticulum (ER), but the exact mechanisms are unknown. We show that double FYVE domain-containing protein 1, a PI(3) P-binding protein with unusual localization on ER and Golgi membranes, translocates in response to amino acid starvation to a punctate compartment partially colocalized with autophagosomal proteins. Translocation is dependent on Vps34 and beclin function. Other PI(3) P-binding probes targeted to the ER show the same starvation-induced translocation that is dependent on PI(3) P formation and recognition. Live imaging experiments show that this punctate compartment forms near Vps34-containing vesicles, is in dynamic equilibrium with the ER, and provides a membrane platform for accumulation of autophagosomal proteins, expansion of autophagosomal membranes, and emergence of fully formed autophagosomes. This PI(3) P-enriched compartment may be involved in autophagosome biogenesis. Its dynamic relationship with the ER is consistent with the idea that the ER may provide important components for autophagosome formation.
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