rdf:type |
|
lifeskim:mentions |
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pubmed:issue |
18
|
pubmed:dateCreated |
2006-8-1
|
pubmed:abstractText |
Synphilin-1 is an alpha-synuclein binding protein that is involved in the pathogenesis of Parkinson's disease. The present study investigated the phospholipid-binding capacity of Synphilin-1. The C-terminus of Synphilin-1 was found to selectively bind to acidic phospholipids, including phosphatidic acid, phosphatidylserine, and phosphatidylglycerol, but not to naturally charged phospholipids. Synphilin-1 was targeted to cytoplasmic lipid droplets in mammalian cells. The amino acid sequence 610-640 was found to represent the primary determinant site for phospholipid binding. Moreover, the R621C mutation identified in Parkinson's disease abolished Synphilin-1 association with lipid droplets. The lipophilicity of Synphilin-1 might prove relevant to its physiologic function.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Aug
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
7
|
pubmed:volume |
580
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4479-84
|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16860793-Animals,
pubmed-meshheading:16860793-Binding Sites,
pubmed-meshheading:16860793-COS Cells,
pubmed-meshheading:16860793-Carrier Proteins,
pubmed-meshheading:16860793-Cercopithecus aethiops,
pubmed-meshheading:16860793-Humans,
pubmed-meshheading:16860793-Lipids,
pubmed-meshheading:16860793-Nerve Tissue Proteins,
pubmed-meshheading:16860793-Phosphatidic Acids,
pubmed-meshheading:16860793-Phosphatidylserines,
pubmed-meshheading:16860793-Phospholipids
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pubmed:year |
2006
|
pubmed:articleTitle |
Interactions of Synphilin-1 with phospholipids and lipid membranes.
|
pubmed:affiliation |
Department of Clinical Neuroscience and Therapeutics, Hiroshima University Graduate School of Biomedical Sciences, 1-2-3 Kasumi, Hiroshima 734-8551, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|