The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Monomeric Synucleins Generate Membrane Curvature
Open accessAbstract
Synucleins are a family of presynaptic membrane binding proteins. α-Synuclein, the principal member of this family, is mutated in familial Parkinson disease. To gain insight into the molecular functions of synucleins, we performed an unbiased proteomic screen and identified synaptic protein changes in αβγ-synuclein knock-out brains. We observed increases in the levels of select membrane curvature sensing/generating proteins. One of the most prominent changes was for the N-BAR protein endophilin A1. Here we demonstrate that the levels of synucleins and endophilin A1 are reciprocally regulated and that they are functionally related. We show that all synucleins can robustly generate membrane curvature similar to endophilins. However, only monomeric but not tetrameric α-synuclein can bend membranes. Further, A30P α-synuclein, a Parkinson disease mutant that disrupts protein folding, is also deficient in this activity. This suggests that synucleins generate membrane curvature through the asymmetric insertion of their N-terminal amphipathic helix. Based on our findings, we propose to include synucleins in the class of amphipathic helix-containing proteins that sense and generate membrane curvature. These results advance our understanding of the physiological function of synucleins. Background: α-Synuclein is a protein of unknown function that is critical for Parkinson disease pathology. Results: All members of the synuclein family can bend membranes when monomeric. Conclusion: Synucleins function at the presynaptic terminal to facilitate membrane curvature generation during synaptic vesicle exo- and endocytosis. Significance: Elucidating synuclein function is important for understanding vesicle trafficking and synaptic dysfunction in Parkinson disease.
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Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
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“While the tetrameric form of -synuclein also binds acidic lipid membranes (16), it is not known if binding is membrane curvature-dependent.”
BackgroundInfluentialCurvature of clathrin-coated pits driven by epsin
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A soluble α-synuclein construct forms a dynamic tetramer
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Cited by
Bendor, J. T., Logan, T. P., & Edwards, R. H. (2013) · Neuron · doi:10.1016/j.neuron.2013.09.004 · Cited by 825
The bowel and beyond: The enteric nervous system in neurological disorders
Rao, M., & Gershon, M. D. (2016) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2016.107 · Cited by 629
α-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson’s disease
Di Maio, R., Barrett, P. J., Hoffman, E. K., Barrett, C. W., Zharikov, A., Borah, A., Hu, X., McCoy, J., Chu, C. T., Burton, E. A., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf3634 · Cited by 619
Cell Biology and Pathophysiology of α-Synuclein
Burré, J., Sharma, M., & Südhof, T. C. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024091 · Cited by 579
The Synaptic Function of α-Synuclein
Burré, J. (2015) · Journal of Parkinson's Disease · doi:10.3233/jpd-150642 · Cited by 573
Metadata
- Authors
- Westphal, C. H., & Chandra, S. S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-01
- Volume
- 288
- Issue
- 3
- Pages
- 1829-1840
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2074167854
- Cited by
- 199
- References
- 10
- FWCI
- 7.48
- Type
- journal article
- Language
- en
- Open access
- hybrid
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