Synucleins in Neurodegeneration
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Neurobiology".
Deadline for manuscript submissions: closed (31 December 2023) | Viewed by 9728
Special Issue Editors
Interests: Parkinson's disease; multiple system atrophy; dementia with Lewy bodies; alpha-synuclein; small ubiquitin-like modifier (SUMO); metallothionein; neuroinflammation; calcium; copper; autophagy
Special Issues, Collections and Topics in MDPI journals
Interests: intrinsically disordered proteins; protein folding; protein misfolding; partially folded proteins; protein aggregation; protein structure; protein function; protein stability; protein biophysics; protein bioinformatics; conformational diseases; protein–ligand interactions; protein–protein interactions; liquid-liquid phase transitions
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
α-synuclein plays a pivotal role in the development of multiple neurodegenerative diseases that are known collectively as synucleinopathies and include Parkinson’s disease, dementia with Lewy bodies, and multiple system atrophy. For many years, research has focused on the formation of intracellular aggregates of protein as the principal causative link to neurodegeneration. Recent studies have revealed many diverse intra- and extracellular neurotoxic interactions, encompassing imbalance in proteostatic systems, metal ion dyshomeostasis, liquid–liquid phase separation, secretory pathway, and mitochondrial dynamics. Although α-synuclein is expressed in multiple different cell types throughout the body, the normal functions of the protein at the neuronal pre-synapse regulating neurotransmitter vesicle trafficking have received much attention and no doubt contribute to the loss of function effects. Emerging data also suggest the extracellular role of α-synuclein as a secreted protein or processed peptide in neuroinflammation that interacts with other disease-linked extracellular proteins, such as tau and Aβ. Central to the normal and pathological activities of α-synuclein is the dynamic nature of the protein that is modulated by calcium-binding, interaction with various partners, and a variety of post-translational modifications. Self-association of α-synuclein in oligomeric, pre-fibrillar, and fibrillar forms provides platforms for the interaction of α-synuclein with a growing array of proteins, lipids, small molecules, and ions. Altogether, α-synuclein, with its spatiotemporal structural heterogeneity and multifunctionality represents an important example of the protein structure–function continuum concept. Furthermore, the potential roles of other members of synuclein family, i.e., β- and γ-synucleins, in normal and pathological processes are becoming obvious. The design of novel neuroprotective and ameliorative therapies requires a comprehensive understanding of the interactome network of the synuclein family members in order to tackle both the initiation and progression of disease processes. In this Special Issue, we hope that investigators will join together in exploring and integrating our current knowledge to stimulate future inquiry towards the goal of disease mitigation.
Dr. Dean L. Pountney
Prof. Dr. Vladimir N. Uversky
Guest Editors
Manuscript Submission Information
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Keywords
- α-synuclein
- β-synuclein
- γ-Synuclein
- Parkinson’s disease
- dementia with Lewy bodies
- multiple system atrophy
- proteostasis
- protein misfolding
- protein–protein interactions
- posttranslational modifications
- disordered proteins
- mitochondria
- autophagy
- neuroinflammation
