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Biomolecules
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Synuclein Proteins II
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Synuclein Proteins II

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 31 August 2024 | Viewed by 7384

Special Issue Editors

Dr. Declan P. McKernan

E-Mail Website
Guest Editor
Pharmacology & Therapeutics, National University of Ireland, H91 W5P7 Galway, Ireland
Interests: neuroinflammation; pattern recognition receptors; schizophrenia
Special Issues, Collections and Topics in MDPI journals
Dr. Xiaobo Mao

E-Mail Website
Guest Editor
Department of Neurology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
Interests: Parkinson's disease; Alzheimer's disease; alpha-synuclein; tau; LAG3; prion-like protein
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues, 

Following a very successful first run, we are pleased to announce the launch of a second edition of the Special Issue on Synuclein Proteins. 

Synucleins are a family of small, soluble proteins expressed in vertebrates whose members include α-synuclein, β-synuclein, and γ-synuclein. All synucleins have a conserved α-helical lipid-binding motif similar to those of apolipoproteins. The α- and β-synuclein proteins are found primarily in brain tissue, where they are seen mainly in presynaptic terminals. The γ-synuclein protein is found primarily in the peripheral nervous system and retina, but also in breast tumors. Cellular functions of the synuclein proteins vary, with data suggesting a common role in the regulation of membrane stability. They have also been demonstrated to form aggregates. Recently, roles in tumor progression and neurodegeneration have been described. Mutations in α-synuclein are associated with rare familial cases of early-onset Parkinson’s disease, and the protein accumulates abnormally, forming part of Lewy bodies in Parkinson’s disease and several other neurodegenerative illnesses. This Special Issue seeks to understand the normal cellular function of these proteins and how they might contribute to the development of human disease. Original manuscripts and reviews dealing with any aspect of synucleins and related pathophysiology are very welcome.

Dr. Declan P. McKernan
Dr. Xiaobo Mao
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • synuclein native structures & functions
  • synuclein genetics
  • tissue expression and regulation of synucleins
  • synuclein aggregates
  • animal models of synucleinopathies
  • synuclein interacting partners
  • synuclein and neurotransmission
  • synuclein and neurodegeneration
  • synuclein and immune responses

Related Special Issue

Published Papers (4 papers)

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Research

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15 pages, 5518 KiB  
Article
The α-Synuclein Monomer May Have Different Misfolding Mechanisms in the Induction of α-Synuclein Fibrils with Different Polymorphs
by Nannan Zhao, Qianqian Zhang, Fansen Yu, Xiaojun Yao and Huanxiang Liu
Biomolecules 2023, 13(4), 682; https://doi.org/10.3390/biom13040682 - 17 Apr 2023
Viewed by 1200
Abstract
The aggregation of alpha-synuclein (α-Syn) is closely related to the occurrence of some neurodegenerative diseases such as Parkinson’s disease. The misfolding of α-Syn monomer plays a key role in the formation of aggregates and extension of fibril. However, the misfolding mechanism of α-Syn [...] Read more.
The aggregation of alpha-synuclein (α-Syn) is closely related to the occurrence of some neurodegenerative diseases such as Parkinson’s disease. The misfolding of α-Syn monomer plays a key role in the formation of aggregates and extension of fibril. However, the misfolding mechanism of α-Syn remains elusive. Here, three different α-Syn fibrils (isolated from a diseased human brain, generated by in vitro cofactor-tau induction, and obtained by in vitro cofactor-free induction) were selected for the study. The misfolding mechanisms of α-Syn were uncovered by studying the dissociation of the boundary chains based on the conventional molecular dynamics (MD) and Steered MD simulations. The results showed that the dissociation paths of the boundary chains in the three systems were different. According to the reverse process of dissociation, we concluded that in the human brain system, the binding of the monomer and template starts from the C-terminal and gradually misfolds toward the N-terminal. In the cofactor-tau system, the monomer binding starts from residues 58–66 (contain β3), followed by the C-terminal coil (residues 67–79). Then, the N-terminal coil (residues 36–41) and residues 50–57 (contain β2) bind to the template, followed by residues 42–49 (contain β1). In the cofactor-free system, two misfolding paths were found. One is that the monomer binds to the N/C-terminal (β1/β6) and then binds to the remaining residues. The other one is that the monomer binds sequentially from the C- to N-terminal, similar to the human brain system. Furthermore, in the human brain and cofactor-tau systems, electrostatic interactions (especially from residues 58–66) are the main driving force during the misfolding process, whereas in the cofactor-free system, the contributions of electrostatic and van der Waals interactions are comparable. These results may provide a deeper understanding for the misfolding and aggregation mechanism of α-Syn. Full article
(This article belongs to the Special Issue Synuclein Proteins II)
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19 pages, 2829 KiB  
Article
Copper Binding and Redox Activity of α-Synuclein in Membrane-Like Environment
by Chiara Bacchella, Francesca Camponeschi, Paulina Kolkowska, Arian Kola, Isabella Tessari, Maria Camilla Baratto, Marco Bisaglia, Enrico Monzani, Luigi Bubacco, Stefano Mangani, Luigi Casella, Simone Dell’Acqua and Daniela Valensin
Biomolecules 2023, 13(2), 287; https://doi.org/10.3390/biom13020287 - 03 Feb 2023
Cited by 4 | Viewed by 1862
Abstract
α-Synuclein (αSyn) constitutes the main protein component of Lewy bodies, which are the pathologic hallmark in Parkinson’s disease. αSyn is unstructured in solution but the interaction of αSyn with lipid membrane modulates its conformation by inducing an α-helical structure of the N-terminal [...] Read more.
α-Synuclein (αSyn) constitutes the main protein component of Lewy bodies, which are the pathologic hallmark in Parkinson’s disease. αSyn is unstructured in solution but the interaction of αSyn with lipid membrane modulates its conformation by inducing an α-helical structure of the N-terminal region. In addition, the interaction with metal ions can trigger αSyn conformation upon binding and/or through the metal-promoted generation of reactive oxygen species which lead to a cascade of structural alterations. For these reasons, the ternary interaction between αSyn, copper, and membranes needs to be elucidated in detail. Here, we investigated the structural properties of copper-αSyn binding through NMR, EPR, and XAS analyses, with particular emphasis on copper(I) coordination since the reduced state is particularly relevant for oxygen activation chemistry. The analysis was performed in different membrane model systems, such as micellar sodium dodecyl sulfate (SDS) and unilamellar vesicles, comparing the binding of full-length αSyn and N-terminal peptide fragments. The presence of membrane-like environments induced the formation of a copper:αSyn = 1:2 complex where Cu+ was bound to the Met1 and Met5 residues of two helical peptide chains. In this coordination, Cu+ is stabilized and is unreactive in the presence of O2 in catechol substrate oxidation. Full article
(This article belongs to the Special Issue Synuclein Proteins II)
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20 pages, 5822 KiB  
Article
Age-Related Changes of the Synucleins Profile in the Mouse Retina
by Sarah Batista Dias, Luísa de Lemos, Luís Sousa, Diogo B. Bitoque, Gabriela Araújo Silva, Miguel C. Seabra and Sandra Tenreiro
Biomolecules 2023, 13(1), 180; https://doi.org/10.3390/biom13010180 - 15 Jan 2023
Viewed by 2392
Abstract
Alpha-synuclein (aSyn) plays a central role in Parkinson’s disease (PD) and has been extensively studied in the brain. This protein is part of the synuclein family, which is also composed of beta-synuclein (bSyn) and gamma-synuclein (gSyn). In addition to its neurotoxic role, synucleins [...] Read more.
Alpha-synuclein (aSyn) plays a central role in Parkinson’s disease (PD) and has been extensively studied in the brain. This protein is part of the synuclein family, which is also composed of beta-synuclein (bSyn) and gamma-synuclein (gSyn). In addition to its neurotoxic role, synucleins have important functions in the nervous system, modulating synaptic transmission. Synucleins are expressed in the retina, but they have been poorly characterized. However, there is evidence that they are important for visual function and that they can play a role in retinal degeneration. This study aimed to profile synucleins in the retina of naturally aged mice and to correlate their patterns with specific retinal cells. With aging, we observed a decrease in the thickness of specific retinal layers, accompanied by an increase in glial reactivity. Moreover, the aSyn levels decreased, whereas bSyn increased with aging. The colocalization of both proteins was decreased in the inner plexiform layer (IPL) of the aged retina. gSyn presented an age-related decrease at the inner nuclear layer but was not significantly changed in the ganglion cell layer. The synaptic marker synaptophysin was shown to be preferentially colocalized with aSyn in the IPL with aging. At the same time, aSyn was found to exist at the presynaptic endings of bipolar cells and was affected by aging. Overall, this study suggests that physiological aging can be responsible for changes in the retinal tissue, implicating functional alterations that could affect synuclein family function. Full article
(This article belongs to the Special Issue Synuclein Proteins II)
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Review

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17 pages, 3065 KiB  
Review
Synuclein Proteins in Cancer Development and Progression
by Lucía C. Zanotti, Florencia Malizia, Nahuel Cesatti Laluce, Aylén Avila, Macarena Mamberto, Luciano E. Anselmino and Mauricio Menacho-Márquez
Biomolecules 2023, 13(6), 980; https://doi.org/10.3390/biom13060980 - 12 Jun 2023
Cited by 2 | Viewed by 1403
Abstract
Synucleins are a family of small, soluble proteins mainly expressed in neural tissue and in certain tumors. Since their discovery, tens of thousands of scientific reports have been published about this family of proteins as they are associated with severe human diseases. Although [...] Read more.
Synucleins are a family of small, soluble proteins mainly expressed in neural tissue and in certain tumors. Since their discovery, tens of thousands of scientific reports have been published about this family of proteins as they are associated with severe human diseases. Although the physiological function of these proteins is still elusive, their relationship with neurodegeneration and cancer has been clearly described over the years. In this review, we summarize data connecting synucleins and cancer, going from the structural description of these molecules to their involvement in tumor-related processes, and discuss the putative use of these proteins as cancer molecular biomarkers. Full article
(This article belongs to the Special Issue Synuclein Proteins II)
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