Abstract:
:Intracellular membrane fusion proceeds via distinct stages of membrane docking, hemifusion and fusion pore opening and depends on interacting families of Rab, SNARE and SM proteins. Trans-SNARE complexes dock the membranes in close apposition. Efficient fusion requires further SNARE-associated proteins. They might increase the number of trans-SNARE complexes or the fusogenic potential of a single SNARE complex. We investigated the contributions of the SM protein Vps33 to hemifusion and pore opening between yeast vacuoles. Mutations in Vps33 that weaken its interactions with the SNARE complex allowed normal trans-SNARE pairing and lipid mixing but retarded content mixing. Deleting the H(abc) domain of the vacuolar t-SNARE Vam3, which interacts with Vps33, had the same effect. This suggests that SM proteins promote fusion pore opening by enhancing the fusogenic activity of a SNARE complex. They should thus be considered integral parts of the fusion machinery.
journal_name
Nat Struct Mol Bioljournal_title
Nature structural & molecular biologyauthors
Pieren M,Schmidt A,Mayer Adoi
10.1038/nsmb.1809subject
Has Abstractpub_date
2010-06-01 00:00:00pages
710-7issue
6eissn
1545-9993issn
1545-9985pii
nsmb.1809journal_volume
17pub_type
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