A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1.
Cell
; 139(6): 1119-29, 2009 Dec 11.
Article
en En
| MEDLINE
| ID: mdl-20005805
ABSTRACT
Vesicle trafficking requires membrane fusion, mediated by SNARE proteins, and upstream events that probably include "tethering," an initial long-range attachment between a vesicle and its target organelle. Among the factors proposed to mediate tethering are a set of multisubunit tethering complexes (MTCs). The Dsl1 complex, with only three subunits, is the simplest known MTC and is essential for the retrograde traffic of COPI-coated vesicles from the Golgi to the ER. To elucidate structural principles underlying MTC function, we have determined the structure of the Dsl1 complex, revealing a tower containing at its base the binding sites for two ER SNAREs and at its tip a flexible lasso for capturing vesicles. The Dsl1 complex binds to individual SNAREs via their N-terminal regulatory domains and also to assembled SNARE complexes; moreover, it is capable of accelerating SNARE complex assembly. Our results suggest that even the simplest MTC may be capable of orchestrating vesicle capture, uncoating, and fusion.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
/
Vesículas Transportadoras
/
Proteínas de Saccharomyces cerevisiae
Idioma:
En
Revista:
Cell
Año:
2009
Tipo del documento:
Article
País de afiliación:
Estados Unidos