Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex

Membrane fusion within the eukaryotic endomembrane system depends on the initial recognition of Rab GTPase on transport vesicles by multisubunit tethering complexes and subsequent coupling to SNARE-mediated fusion. The conserved vacuolar/lysosomal homotypic fusion and vacuole protein sorting (HOPS)...

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Published in:Proceedings of the National Academy of Sciences - PNAS 2012-02, Vol.109 (6), p.1991-1996
Main Authors: Bröcker, Cornelia, Kuhlee, Anne, Gatsogiannis, Christos, Balderhaar, Henning J. kleine, Hönscher, Carina, Engelbrecht-Vandré, Siegfried, Ungermann, Christian, Raunser, Stefan
Format: Article
Language:English
Subjects:
Antibodies
Architecture
Binding Sites
Biological Sciences
Cogs
Endosomes
Eukaryotes
Experimental procedures
Green Fluorescent Proteins - metabolism
Lipids
Membrane Fusion
Membranes
Molecular structure
Multiprotein Complexes - chemistry
Multiprotein Complexes - isolation & purification
Multiprotein Complexes - metabolism
Multiprotein Complexes - ultrastructure
P branes
Protein Binding
Protein Subunits - chemistry
Protein Subunits - metabolism
Protein Transport
Proteins
rab GTP-Binding Proteins - metabolism
Recombinant Fusion Proteins - metabolism
Static Electricity
Vacuoles
Vacuoles - metabolism
Yeasts
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Summary:Membrane fusion within the eukaryotic endomembrane system depends on the initial recognition of Rab GTPase on transport vesicles by multisubunit tethering complexes and subsequent coupling to SNARE-mediated fusion. The conserved vacuolar/lysosomal homotypic fusion and vacuole protein sorting (HOPS) tethering complex combines both activities. Here we present the overall structure of the fusion-active HOPS complex. Our data reveal a flexible ≈30-nm elongated seahorse-like structure, which can adopt contracted and elongated shapes. Surprisingly, both ends of the HOPS complex contain a Rab-binding subunit: Vps41 and Vps39. The large head contains in addition to Vps41 the SNARE-interacting Vps33, whereas Vps39 is found in the bulky tip of its tail. Vps11 and Vps18 connect head and tail. Our data suggest that HOPS bridges Ypt7-positive membranes and chaperones SNAREs at fusion sites.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1117797109