Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.mcn.2010.07.014
Title: EHD1 is a synaptic protein that modulates exocytosis through binding to snapin
Authors: Wei, S.
Xu, Y.
Shi, H.
Wong, S.-H. 
Han, W.
Talbot, K.
Hong, W.
Ong, W.-Y.
Keywords: Axons
EHD1
Exocytosis
Neurons
SNAP-25
Snapin
SNAREs
Synapse
Synaptic vesicles
Issue Date: Dec-2010
Citation: Wei, S., Xu, Y., Shi, H., Wong, S.-H., Han, W., Talbot, K., Hong, W., Ong, W.-Y. (2010-12). EHD1 is a synaptic protein that modulates exocytosis through binding to snapin. Molecular and Cellular Neuroscience 45 (4) : 418-429. ScholarBank@NUS Repository. https://doi.org/10.1016/j.mcn.2010.07.014
Abstract: EHD1 is an EH (Eps15 homology) domain-containing protein involved in endosomal recycling. Our yeast two hybrid screening experiments showed that EHD1 interacts with a synaptic protein, snapin, and the present study was carried out to further elucidate the functional significance of this interaction. Immunoreactivity to EHD1 is observed in the cerebral cortex, hippocampus and striatum, in the rat brain. The protein is colocalized with the axon terminal marker synaptophysin in cultured neurons. EHD1 binds to the C terminus of snapin via its C terminus EH domain. It negatively affects the binding of a SNARE complex protein, SNAP-25, to snapin, probably due to the competition for overlapping binding sites on the C terminus of snapin. EHD1 affects the coupling of synaptotagmin-1 to the SNARE complex, and could be a negative regulator of exocytosis. This is supported by electrophysiological findings that PC-12 cells which overexpress EHD1 show reduced depolarization-induced exocytosis compared to controls, but the reduced exocytosis is not observed in cells which overexpress the N terminus of EHD1 that is unable to bind snapin. Together, the above results indicate that EHD1 is a synaptic protein that negatively affects exocytosis through binding to snapin. © 2010 Elsevier Inc.
Source Title: Molecular and Cellular Neuroscience
URI: http://scholarbank.nus.edu.sg/handle/10635/108359
ISSN: 10447431
DOI: 10.1016/j.mcn.2010.07.014
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