A novel in vitro assay reveals SNARE topology and the role of Ykt6 in autophagosome fusion with vacuoles

Autor(en): Gao, Jieqiong
Reggiori, Fulvio
Ungermann, Christian 
Stichwörter: Cell Biology; EFFECTOR COMPLEX; HOPS CATALYZES; MEMBRANE-TRANSPORT PATHWAYS; MONITORING AUTOPHAGY; NUCLEOTIDE EXCHANGE; PROTEIN PALMITOYLATION; RAB GTPASE; SACCHAROMYCES-CEREVISIAE; SYNTAXIN 17; TETHERING COMPLEX
Erscheinungsdatum: 2018
Herausgeber: ROCKEFELLER UNIV PRESS
Journal: JOURNAL OF CELL BIOLOGY
Volumen: 217
Ausgabe: 10
Startseite: 3670
Seitenende: 3682
Zusammenfassung: 
Autophagy is a catabolic pathway that delivers intracellular material to the mammalian lysosomes or the yeast and plant vacuoles. The final step in this process is the fusion of autophagosomes with vacuoles, which requires SNARE proteins, the homotypic vacuole fusion and protein sorting tethering complex, the RAB7-like Ypt7 GTPase, and its guanine nucleotide exchange factor, Mon1-Ccz1. Where these different components are located and function during fusion, however, remains to be fully understood. Here, we present a novel in vitro assay to monitor fusion of intact and functional autophagosomes with vacuoles. This process requires ATP, physiological temperature, and the entire fusion machinery to tether and fuse autophagosomes with vacuoles. Importantly, we uncover Ykt6 as the autophagosomal SNARE. Our assay and findings thus provide the tools to dissect autophagosome completion and fusion in a test tube.
ISSN: 00219525
DOI: 10.1083/jcb.201804039

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