Interactions of Synphilin-1 with phospholipids and lipid membranes |
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Authors: | Takahashi Tetsuya Yamashita Hiroshi Nagano Yoshito Nakamura Takeshi Kohriyama Tatsuo Matsumoto Masayasu |
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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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Abstract: | 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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Keywords: | Synphilin-1 α-Synuclein Parkinson’s disease Phospholipid Lipid droplet |
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