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

Autor(en): Broecker, Cornelia
Kuhlee, Anne
Gatsogiannis, Christos
Balderhaar, Henning J. Kleine
Hoenscher, Carina
Engelbrecht-Vandre, Siegfried
Ungermann, Christian 
Raunser, Stefan
Stichwörter: DOCKING; DOMAIN; GTPASE; INTERACTS; MEMBRANE-FUSION; Multidisciplinary Sciences; PHOSPHORYLATION; Science & Technology - Other Topics; SNARE COMPLEX; SUBUNIT; VESICLE COATS; VISUALIZATION
Erscheinungsdatum: 2012
Herausgeber: NATL ACAD SCIENCES
Journal: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volumen: 109
Ausgabe: 6
Startseite: 1991
Seitenende: 1996
Zusammenfassung: 
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 approximate to 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: 00278424
DOI: 10.1073/pnas.1117797109

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