Journal
TRAFFIC
Volume 10, Issue 2, Pages 218-234Publisher
WILEY
DOI: 10.1111/j.1600-0854.2008.00853.x
Keywords
alpha-synuclein; clathrin-mediated endocytosis; membrane fluidity; membrane trafficking; Parkinson's disease; polyunsaturated fatty acids; synaptic vesicle recycling
Categories
Funding
- National Institute of Neurological Disorders and Stroke (NINDS) [R01 NS051318]
Ask authors/readers for more resources
alpha-Synuclein (alpha S) 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, alpha S can reversibly associate with membranes and help regulate membrane fatty acid composition. We previously observed that variations in alpha S 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 alpha S acts with PUFAs to enhance the internalization of the membrane-binding dye, FM 1-43. Specifically, alpha S expression coupled with exposure to physiological levels of certain PUFAs enhanced clathrin-mediated endocytosis in neuronal and non-neuronal cultured cells. Moreover, alpha S expression and PUFA-enhanced basal and -evoked synaptic vesicle (SV) endocytosis in primary hippocampal cultures of wild type (wt) and genetically depleted alpha S mouse brains. We suggest that alpha S and PUFAs normally function in endocytic mechanisms and are specifically involved in SV recycling upon neuronal stimulation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available