The Sybtraps: Control of Synaptobrevin Traffic by Synaptophysin, α-Synuclein and AP-180
Article first published online: 16 DEC 2013
© 2013 The Authors. Traffic published by John Wiley & Sons Ltd.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Volume 15, Issue 3, pages 245–254, March 2014
How to Cite
Gordon, S. L. and Cousin, M. A. (2014), The Sybtraps: Control of Synaptobrevin Traffic by Synaptophysin, α-Synuclein and AP-180. Traffic, 15: 245–254. doi: 10.1111/tra.12140
- Issue published online: 10 FEB 2014
- Article first published online: 16 DEC 2013
- Accepted manuscript online: 26 NOV 2013 10:25AM EST
- Manuscript Accepted: 26 NOV 2013
- Manuscript Revised: 22 NOV 2013
- Manuscript Received: 16 OCT 2013
- Wellcome Trust. Grant Number: 088138
Synaptobrevin 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.