Journal
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, VOL 26
Volume 26, Issue -, Pages 115-136Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-cellbio-100109-104131
Keywords
priming; docking; membrane microdomain
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Funding
- NIGMS NIH HHS [R01 GM023377] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM023377] Funding Source: NIH RePORTER
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Although fusion mechanisms are highly conserved in evolution and among organelles of the exocytic and endocytic pathways, yeast vacuole homotypic fusion offers unique technical advantages: excellent genetics, clear organelle cytology, in vitro colorimetric fusion assays, and reconstitution of fusion from all-pure components, including a Rab GTPase, HOPS (homotypic fusion and vacuole protein sorting complex), four SNAREs [soluble N-ethylmaleimide-sensitive factor (NSF) attachment receptors] that snare (bind)each other, SNARE-complex disassembly chaperones, and vacuolar lipids. Vacuole fusion studies offer paradigms of the interdependence of lipids and fusion proteins to assemble a fusion microdomain, distinct lipid functions, SNARE complex proofreading through the synergy between HOPS and the SNARE disassembly chaperones, and the role of each fusion protein in promoting radical bilayer restructuring for fusion without lysis.
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