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Regulation of Synaptic Vesicle Budding and Dynamin Function by an EHD ATPase
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Pharmacology.
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2011 (English)In: Journal of Neuroscience, ISSN 0270-6474, E-ISSN 1529-2401, Vol. 31, no 39, 13972-13980 p.Article in journal (Refereed) Published
Abstract [en]

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 (1-EHD) in the lamprey giant reticulospinal synapse. 1-EHD was detected by immunogold at endocytic structures adjacent to release sites. In antibody microinjection experiments, perturbation of 1-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 1-EHD directly interferes with dynamin function, we used fluid-supported bilayers as in vitro assay. We found that 1-EHD strongly inhibited vesicle budding induced by dynamin in the constant presence of GTP. 1-EHD also inhibited dynamin-induced membrane tubulation in the presence of GTP gamma S, a phenomenon linked with dynamin helix assembly. Our in vivo results demonstrate the involvement of 1-EHD in clathrin/dynamin-dependent synaptic vesicle budding. Based on our in vitro observations, we suggest that 1-EHD acts to limit the formation of long, unproductive dynamin helices, thereby promoting vesicle budding.

Place, publisher, year, edition, pages
2011. Vol. 31, no 39, 13972-13980 p.
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Medical and Health Sciences
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URN: urn:nbn:se:uu:diva-160404DOI: 10.1523/JNEUROSCI.1289-11.2011ISI: 000295363800028OAI: oai:DiVA.org:uu-160404DiVA: diva2:450937
Available from: 2011-10-24 Created: 2011-10-24 Last updated: 2017-12-08Bibliographically approved

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