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-Structure paper
Title | Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 109, Issue 6, Page 1991-1996, Year 2012 |
Publish date | Feb 7, 2012 |
Authors | Cornelia Bröcker / Anne Kuhlee / Christos Gatsogiannis / Henning J kleine Balderhaar / Carina Hönscher / Siegfried Engelbrecht-Vandré / Christian Ungermann / Stefan Raunser / |
PubMed Abstract | 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- ...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. |
External links | Proc Natl Acad Sci U S A / PubMed:22308417 / PubMed Central |
Methods | EM (single particle) |
Resolution | 30.4 Å |
Structure data | EMDB-2280: |
Source |
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