Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid
- PMID: 10490020
- DOI: 10.1038/43613
Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid
Abstract
Endophilin I is a presynaptic protein of unknown function that binds to dynamin, a GTPase that is implicated in endocytosis and recycling of synaptic vesicles. Here we show that endophilin I is essential for the formation of synaptic-like microvesicles (SLMVs) from the plasma membrane. Endophilin I exhibits lysophosphatidic acid acyl transferase (LPAAT) activity, and endophilin-I-mediated SLMV formation requires the transfer of the unsaturated fatty acid arachidonate to lysophosphatidic acid, converting it to phosphatidic acid. A deletion mutant lacking the SH3 domain through which endophilin I interacts with dynamin still exhibits LPAAT activity but no longer mediates SLMV formation. These results indicate that endophilin I may induce negative membrane curvature by converting an inverted-cone-shaped lipid to a cone-shaped lipid in the cytoplasmic leaflet of the bilayer. We propose that, through this action, endophilin I works with dynamin to mediate synaptic vesicle invagination from the plasma membrane and fission.
Comment in
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Lipid membranes shape up.Nature. 1999 Sep 9;401(6749):123-4. doi: 10.1038/43582. Nature. 1999. PMID: 10490016 No abstract available.
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