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Interactions of Synphilin‐1 with phospholipids and lipid membranes
Author(s) -
Takahashi Tetsuya,
Yamashita Hiroshi,
Nagano Yoshito,
Nakamura Takeshi,
Kohriyama Tatsuo,
Matsumoto Masayasu
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.07.019
Subject(s) - phosphatidic acid , phospholipid , phosphatidylserine , biochemistry , cardiolipin , phosphatidylglycerol , chemistry , lipophilicity , glycerophospholipid , phosphatidylcholine , membrane , biology , microbiology and biotechnology
Synphilin‐1 is an α‐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.