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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6749
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pubmed:dateCreated |
1999-9-27
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-acylglycerophosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Lysophospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphonic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SH3GL2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sh3gl2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/methyl arachidonylfluorophosphonate
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
401
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
133-41
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10490020-Acyl Coenzyme A,
pubmed-meshheading:10490020-Acyltransferases,
pubmed-meshheading:10490020-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:10490020-Amino Acid Sequence,
pubmed-meshheading:10490020-Animals,
pubmed-meshheading:10490020-Arachidonic Acid,
pubmed-meshheading:10490020-Arachidonic Acids,
pubmed-meshheading:10490020-Carrier Proteins,
pubmed-meshheading:10490020-Cattle,
pubmed-meshheading:10490020-Cell Membrane,
pubmed-meshheading:10490020-Enzyme Inhibitors,
pubmed-meshheading:10490020-Humans,
pubmed-meshheading:10490020-Lysophospholipids,
pubmed-meshheading:10490020-Membrane Fusion,
pubmed-meshheading:10490020-Membrane Lipids,
pubmed-meshheading:10490020-Mice,
pubmed-meshheading:10490020-Models, Biological,
pubmed-meshheading:10490020-Molecular Conformation,
pubmed-meshheading:10490020-Molecular Sequence Data,
pubmed-meshheading:10490020-PC12 Cells,
pubmed-meshheading:10490020-Phospholipases A,
pubmed-meshheading:10490020-Phosphonic Acids,
pubmed-meshheading:10490020-Phosphorylation,
pubmed-meshheading:10490020-Protein Binding,
pubmed-meshheading:10490020-Rats,
pubmed-meshheading:10490020-Recombinant Fusion Proteins,
pubmed-meshheading:10490020-Synaptic Vesicles,
pubmed-meshheading:10490020-src Homology Domains
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pubmed:year |
1999
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pubmed:articleTitle |
Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid.
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pubmed:affiliation |
Max-Planck-Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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