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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geprüft am 29.05.2024