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Brain Sciences
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The Neural Processes Underlying Parkinson’s Disease and Related Synucleinopathies
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The Neural Processes Underlying Parkinson’s Disease and Related Synucleinopathies

A special issue of Brain Sciences (ISSN 2076-3425). This special issue belongs to the section "Neurodegenerative Diseases".

Deadline for manuscript submissions: closed (5 May 2026) | Viewed by 1621

Special Issue Editor

Dr. Danielle E. Mor

E-Mail Website
Guest Editor
Department of Neuroscience and Regenerative Medicine, Medical College of Georgia at Augusta University, Augusta, GA 30912, USA
Interests: Parkinson’s disease and other neurodegenerative disorders; ageing

Special Issue Information

Dear Colleagues,

Understanding the processes underlying neurodegeneration in Parkinson’s disease and related synucleinopathies is critically important for the development of disease-modifying therapeutics. These disorders, which include dementia with Lewy bodies and multiple system atrophy, share the common feature of aggregation of a-synuclein protein into insoluble filamentous inclusions. Despite extensive research efforts, the relationship of protein aggregation with neuronal dysfunction and ultimate demise is yet to be fully understood. Moreover, the mechanisms governing shared versus unique aspects of these disorders requires further investigation.

This Special Issue of Brain Sciences explores the latest discoveries of the disease mechanisms in synucleinopathies. Authors are invited to submit cutting-edge research and reviews on a broad range of topics related to these disorders, including but not limited to a-synuclein cell-to-cell transmission, gut-brain interactions in Parkinson’s disease, and the interplay of a-synuclein with tau and other co-occurring protein pathologies. Collectively, the aim of this issue is to enhance scientific understanding of the complex interactions between protein aggregates and cellular machinery leading to neuron death, in order to highlight new potential avenues for disease treatments.

Dr. Danielle E. Mor
Guest Editor

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 250 words) can be sent to the Editorial Office for assessment.

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. Brain Sciences 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 2200 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

  • α-synuclein
  • synucleinopathies
  • Parkinson’s disease
  • dementia with Lewy bodies
  • multiple system atrophy
  • neurodegeneration
  • protein aggregation

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Published Papers (1 paper)

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Research

18 pages, 3332 KB  
Article
Calpain-2 Regulates Kinesin and Dynein Dysfunction in Neurotoxin-Induced Motoneuron Injury
by Vandana Zaman, Camille Green, Kayce Sitgreaves, Amy Gathings, Kelsey P. Drasites, Noah Coleman, Jessica Huell, Townsend McDonald, Narendra L. Banik and Azizul Haque
Brain Sci. 2026, 16(1), 92; https://doi.org/10.3390/brainsci16010092 - 16 Jan 2026
Viewed by 1063
Abstract
Background/Objectives: Neurodegenerative diseases are driven by multiple interconnected pathological mechanisms involving both intrinsic and extrinsic molecular and cellular processes. Efficient bidirectional intracellular transport is essential for neuronal survival and function, enabling the movement of organelles, proteins, and vesicles between the neuronal soma and [...] Read more.
Background/Objectives: Neurodegenerative diseases are driven by multiple interconnected pathological mechanisms involving both intrinsic and extrinsic molecular and cellular processes. Efficient bidirectional intracellular transport is essential for neuronal survival and function, enabling the movement of organelles, proteins, and vesicles between the neuronal soma and distal compartments. This process is primarily mediated by kinesin-dependent anterograde transport and dynein-dependent retrograde transport. Disruption of either motor protein compromises endosome–lysosome recycling, leading to cellular dysfunction and neurodegeneration. However, the mechanisms underlying motor protein impairment in Parkinson’s disease (PD) remain incompletely understood. Methods: We investigated the involvement of kinesin and dynein in intracellular transport dysfunction using both in vitro and in vivo models of PD. Cultured neuronal cells were exposed to MPP+ (1-methyl-4-phenylpyridinium) to model PD-associated neurotoxicity, and motor protein function, vesicular trafficking, and endosomal recycling were assessed. In parallel, an MPTP (1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine)-induced mouse model of PD was used to evaluate dynein-positive fiber density in the spinal cord. The role of calpain-2 was examined by co-treatment with the selective calpain-2 inhibitor zLLYCH2F in both experimental systems. Results: MPP+ exposure disrupted kinesin- and dynein-mediated transport in neuronal cytoplasm, resulting in impaired vesicular trafficking and defective endosome–lysosome recycling. These alterations led to abnormal accumulation of vesicles in both perinuclear regions and at the cell periphery. Pharmacological inhibition of calpain-2 with zLLYCH2F restored motor protein function and normalized vesicle distribution in MPP+-treated cells. Consistent with in vitro findings, MPTP-treated mice exhibited a significant reduction in dynein-positive fiber density within the spinal cord, which was prevented by co-treatment with zLLYCH2F. Conclusions: Our findings demonstrate that calpain-2 activation contributes to kinesin and dynein dysfunction following MPP+/MPTP exposure, leading to impaired intracellular transport and vesicle recycling in PD models. Inhibition of calpain-2 preserves motor protein function, maintains cytoskeletal integrity, and supports normal intracellular trafficking. These results identify calpain-2 as a critical regulator of motor protein stability and suggest that targeting calpain-2 may represent a promising therapeutic strategy for mitigating intracellular transport defects in Parkinson’s disease. Full article
(This article belongs to the Special Issue The Neural Processes Underlying Parkinson’s Disease and Related Synucleinopathies)
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