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Regulation of Synaptic Vesicle Budding and Dynamin Function by an EHD ATPase

Jakobsson, Joel, Ackermann, Frauke, Andersson, Fredrik, Larhammar, Dan, Löw, Peter, Brodin, Lennart·2011·The Journal of Neuroscience
DOI 10.1523/jneurosci.1289-11.2011
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Abstract

Eps15 homology domain-containing proteins (EHDs) are conserved ATPases implicated in membrane remodeling. Recently, EHD1 was found to be enriched at synaptic release sites, suggesting a possible involvement in the trafficking of synaptic vesicles. We have investigated the role of an EHD1/3 ortholog (l-EHD) in the lamprey giant reticulospinal synapse. l-EHD was detected by immunogold at endocytic structures adjacent to release sites. In antibody microinjection experiments, perturbation of l-EHD inhibited synaptic vesicle endocytosis and caused accumulation of clathrin-coated pits with atypical, elongated necks. The necks were covered with helix-like material containing dynamin. To test whether l-EHD directly interferes with dynamin function, we used fluid-supported bilayers as in vitro assay. We found that l-EHD strongly inhibited vesicle budding induced by dynamin in the constant presence of GTP. l-EHD also inhibited dynamin-induced membrane tubulation in the presence of GTPγS, a phenomenon linked with dynamin helix assembly. Our in vivo results demonstrate the involvement of l-EHD in clathrin/dynamin-dependent synaptic vesicle budding. Based on our in vitro observations, we suggest that l-EHD acts to limit the formation of long, unproductive dynamin helices, thereby promoting vesicle budding.

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Metadata

Authors
Jakobsson, J., Ackermann, F., Andersson, F., Larhammar, D., Löw, P., & Brodin, L.
Venue
The Journal of Neuroscience
Publisher
Society for Neuroscience
Published
2011-09-28
Volume
31
Issue
39
Pages
13972-13980
ISSN
  • 0270-6474
  • 1529-2401
DOI
10.1523/jneurosci.1289-11.2011
Cited by
44
References
2
Language
en
Licence
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 182 d)

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