The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Ca2+ Binding to α-Synuclein Regulates Ligand Binding and Oligomerization
Open accessAbstract
alpha-Synuclein is a protein normally involved in presynaptic vesicle homeostasis. It participates in the development of Parkinson's disease, in which the nerve cell lesions, Lewy bodies, accumulate alpha-synuclein filaments. The synaptic neurotransmitter release is primarily dependent on Ca(2+)-regulated processes. A microdialysis technique was applied showing that alpha-synuclein binds Ca(2+) with an IC(50) of about 2-300 microm and in a reaction uninhibited by a 50-fold excess of Mg(2+). The Ca(2+)-binding site consists of a novel C-terminally localized acidic 32-amino acid domain also present in the homologue beta-synuclein, as shown by Ca(2+) binding to truncated recombinant and synthetic alpha-synuclein peptides. Ca(2+) binding affects the functional properties of alpha-synuclein. First, the ligand binding of (125)I-labeled bovine microtubule-associated protein 1A is stimulated by Ca(2+) ions in the 1-500 microm range and is dependent on an intact Ca(2+) binding site in alpha-synuclein. Second, the Ca(2+) binding stimulates the proportion of (125)I-alpha-synuclein-containing oligomers. This suggests that Ca(2+) ions may both participate in normal alpha-synuclein functions in the nerve terminal and exercise pathological effects involved in the formation of Lewy bodies.
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AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
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Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine System
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A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding.
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α-Synuclein misfolding and Parkinson's disease
Breydo, L., Wu, J. W., & Uversky, V. N. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.002 · Cited by 657
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
Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation
Uversky, V. N. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04764.x · Cited by 567
Hsp70 Reduces α-Synuclein Aggregation and Toxicity
Klucken, J., Shin, Y., Masliah, E., Hyman, B. T., & McLean, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400255200 · Cited by 508
Metadata
- Authors
- Nielsen, M. S., Vorum, H., Lindersson, E., & Jensen, P. H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-06
- Volume
- 276
- Issue
- 25
- Pages
- 22680-22684
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1952199403
- Cited by
- 176
- References
- 6
- FWCI
- 4.42
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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