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Special Issue "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: 30 September 2022 | Viewed by 915

Special Issue Editors

Dr. Dean L. Pountney
E-Mail Website
Guest Editor
School of Medical Science, Griffith University, Gold Coast 4222, Australia
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
Prof. Dr. Vladimir N. Uversky
grade E-Mail Website
Guest Editor
Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA
Interests: proteon physics; protein folding; protein structure; protein function; protein misfolding; protein aggregation; intrinsically disordered proteins; proteinopathies; proteinaceous membrane-less organelles; 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

Published Papers (1 paper)

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Research

Article
SARS-CoV-2 Proteins Interact with Alpha Synuclein and Induce Lewy Body-like Pathology In Vitro
Int. J. Mol. Sci. 2022, 23(6), 3394; https://doi.org/10.3390/ijms23063394 - 21 Mar 2022
Viewed by 683
Abstract
Growing cases of patients reported have shown a potential relationship between (severe acute respiratory syndrome coronavirus 2) SARS-CoV-2 infection and Parkinson’s disease (PD). However, it is unclear whether there is a molecular link between these two diseases. Alpha-synuclein (α-Syn), an aggregation-prone protein, is [...] Read more.
Growing cases of patients reported have shown a potential relationship between (severe acute respiratory syndrome coronavirus 2) SARS-CoV-2 infection and Parkinson’s disease (PD). However, it is unclear whether there is a molecular link between these two diseases. Alpha-synuclein (α-Syn), an aggregation-prone protein, is considered a crucial factor in PD pathology. In this study, bioinformatics analysis confirmed favorable binding affinity between α-Syn and SARS-CoV-2 spike (S) protein and nucleocapsid (N) protein, and direct interactions were further verified in HEK293 cells. The expression of α-Syn was upregulated and its aggregation was accelerated by S protein and N protein. It was noticed that SARS-CoV-2 proteins caused Lewy-like pathology in the presence of α-Syn overexpression. By confirming that SARS-CoV-2 proteins directly interact with α-Syn, our study offered new insights into the mechanism underlying the development of PD on the background of COVID-19. Full article
(This article belongs to the Special Issue Synucleins in Neurodegeneration)
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