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.
journal_name
Naturejournal_title
Natureauthors
Schmidt A,Wolde M,Thiele C,Fest W,Kratzin H,Podtelejnikov AV,Witke W,Huttner WB,Söling HDdoi
10.1038/43613keywords:
subject
Has Abstractpub_date
1999-09-09 00:00:00pages
133-41issue
6749eissn
0028-0836issn
1476-4687journal_volume
401pub_type
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