Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid

Anne Schmidt, Michael Wolde, Christoph Thiele, Werner Fest, Hartmut Kratzin, Alexandre V. Podtelejnikov, Walter Witke, Wieland B. Huttner () and Hans-Dieter Söling ()
Additional contact information
Anne Schmidt: Max-Planck-Institute of Molecular Cell Biology and Genetics
Michael Wolde: University of Göttingen, and Max-Planck-Institute of Biophysical Chemistry
Christoph Thiele: Max-Planck-Institute of Molecular Cell Biology and Genetics
Werner Fest: University of Göttingen, and Max-Planck-Institute of Biophysical Chemistry
Hartmut Kratzin: Max-Planck-Institute for Experimental Medicine
Alexandre V. Podtelejnikov: European Molecular Biology Laboratory
Walter Witke: European Molecular Biology Laboratory
Wieland B. Huttner: Max-Planck-Institute of Molecular Cell Biology and Genetics
Hans-Dieter Söling: University of Göttingen, and Max-Planck-Institute of Biophysical Chemistry

Nature, 1999, vol. 401, issue 6749, 133-141

Abstract: 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.

Date: 1999
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/43613 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:401:y:1999:i:6749:d:10.1038_43613

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/43613

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().