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dc.contributor.authorGordon, SL
dc.contributor.authorCousin, MA
dc.date.accessioned2020-12-10T00:55:36Z
dc.date.available2020-12-10T00:55:36Z
dc.date.issued2014-03
dc.identifier.citationGordon, S. L. & Cousin, M. A. (2014). The Sybtraps: control of synaptobrevin traffic by synaptophysin, α-synuclein and AP-180.. Traffic, 15 (3), pp.245-254. https://doi.org/10.1111/tra.12140.
dc.identifier.issn1398-9219
dc.identifier.urihttp://hdl.handle.net/11343/253609
dc.description.abstractSynaptobrevin II (sybII) is a key fusogenic molecule on synaptic vesicles (SVs) therefore the active maintenance of both its conformation and location in sufficient numbers on this organelle is critical in both mediating and sustaining neurotransmitter release. Recently three proteins have been identified having key roles in the presentation, trafficking and retrieval of sybII during the fusion and endocytosis of SVs. The nerve terminal protein α-synuclein catalyses sybII entry into SNARE complexes, whereas the monomeric adaptor protein AP-180 is required for sybII retrieval during SV endocytosis. Overarching these events is the tetraspan SV protein synaptophysin, which is a major sybII interaction partner on the SV. This review will evaluate recent studies to propose working models for the control of sybII traffic by synaptophysin and other Sybtraps (sybII trafficking partners) and suggest how dysfunction in sybII traffic may contribute to human disease.
dc.languageeng
dc.publisherWiley
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleThe Sybtraps: control of synaptobrevin traffic by synaptophysin, α-synuclein and AP-180.
dc.typeJournal Article
dc.identifier.doi10.1111/tra.12140
melbourne.affiliation.departmentFlorey Department of Neuroscience and Mental Health
melbourne.source.titleTraffic
melbourne.source.volume15
melbourne.source.issue3
melbourne.source.pages245-254
dc.rights.licenseCC BY
melbourne.elementsid1369366
melbourne.openaccess.pmchttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3992847
melbourne.contributor.authorGordon, Sarah
dc.identifier.eissn1600-0854
melbourne.accessrightsOpen Access


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