Subunit connectivity, assembly determinants and architecture of the yeast exocyst complex
Authors
Heider, Margaret R.Gu, Mingyu
Duffy, Caroline M.
Mirza, Anne M.
Marcotte, Laura L.
Walls, Alexandra C.
Farrall, Nicholas
Hakhverdyan, Zhanna
Field, Mark C.
Rout, Michael P.
Frost, Adam
Munson, Mary
Student Authors
Caroline M. Duffy; Margaret R. HeiderUMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyDocument Type
Journal ArticlePublication Date
2016-01-01
Metadata
Show full item recordAbstract
The exocyst is a hetero-octameric complex that has been proposed to serve as the tethering complex for exocytosis, although it remains poorly understood at the molecular level. Here, we purified endogenous exocyst complexes from Saccharomyces cerevisiae and showed that they are stable and consist of all eight subunits with equal stoichiometry. Using a combination of biochemical and auxin induced-degradation experiments in yeast, we mapped the subunit connectivity, identified two stable four-subunit modules within the octamer and demonstrated that several known exocyst-binding partners are not necessary for exocyst assembly and stability. Furthermore, we visualized the structure of the yeast complex by using negative-stain electron microscopy; our results indicate that the exocyst exists predominantly as a stable, octameric complex with an elongated architecture that suggests that the subunits are contiguous helical bundles packed together into a bundle of long rods.Source
Nat Struct Mol Biol. 2016 Jan;23(1):59-66. doi: 10.1038/nsmb.3146. Epub 2015 Dec 14. Link to article on publisher's site
DOI
10.1038/nsmb.3146Permanent Link to this Item
http://hdl.handle.net/20.500.14038/33500PubMed ID
26656853Related Resources
ae974a485f413a2113503eed53cd6c53
10.1038/nsmb.3146