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α‐Synuclein and Polyunsaturated Fatty Acids Promote Clathrin‐Mediated Endocytosis and Synaptic Vesicle Recycling
Author(s) -
Ben Gedalya Tziona,
Loeb Virginie,
Israeli Eitan,
Altschuler Yoram,
Selkoe Dennis J.,
Sharon Ronit
Publication year - 2009
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2008.00853.x
Subject(s) - endocytosis , endocytic cycle , clathrin , biology , internalization , microbiology and biotechnology , synaptic vesicle recycling , polyunsaturated fatty acid , synaptic vesicle , exocytosis , vesicle , biochemistry , fatty acid , cell , membrane
α‐Synuclein (αS) is an abundant neuronal cytoplasmic protein implicated in Parkinson’s disease (PD), but its physiological function remains unknown. Consistent with its having structural motifs shared with class A1 apolipoproteins, αS can reversibly associate with membranes and help regulate membrane fatty acid composition. We previously observed that variations in αS expression level in dopaminergic cultured cells or brains are associated with changes in polyunsaturated fatty acid (PUFA) levels and altered membrane fluidity. We now report that αS acts with PUFAs to enhance the internalization of the membrane‐binding dye, FM 1‐43. Specifically, αS expression coupled with exposure to physiological levels of certain PUFAs enhanced clathrin‐mediated endocytosis in neuronal and non‐neuronal cultured cells. Moreover, αS expression and PUFA‐enhanced basal and ‐evoked synaptic vesicle (SV) endocytosis in primary hippocampal cultures of wild type (wt) and genetically depleted αS mouse brains. We suggest that αS and PUFAs normally function in endocytic mechanisms and are specifically involved in SV recycling upon neuronal stimulation.