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Phosphorylation, Dephosphorylation, and Multiprotein Assemblies Regulate Dynamic Behavior of Neuronal Cytoskeleton: A
Natalya Kurochkina1, Manju Bhaskar2, Sharda Prasad Yadav2
1Department of Biophysics, The School of Theoretical Modeling, Washington, DC, United States.
Frontiers in Molecular Neuroscience
|October 24, 2018
Summary
Phosphorylation regulates neurofilament assembly and aggregation, crucial in neurodegenerative diseases like Alzheimer's. Aberrant tau protein accumulation in cell bodies, unlike healthy axonal localization, drives disease progression.
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- Neurofilaments and neuronal protein tau are key to neuronal function.
- Phosphorylation critically regulates tau's cellular localization, assembly, and aggregation.
- Aberrant tau accumulation is implicated in Alzheimer's disease, Parkinson's disease, and ALS.
Purpose of the Study:
- To review the role of phosphorylation in neurofilament and tau dynamics.
- To discuss aberrant spatial distribution of neuronal polypeptides in neuropathies.
- To highlight advancements in understanding Alzheimer's disease pathogenesis and therapeutic targets.
Main Methods:
- Literature review focusing on phosphorylation, neurofilaments, and tau.
- Analysis of protein aggregation and cellular localization in neurodegeneration.
- Exploration of epigenetic factors and proteomics in Alzheimer's disease.
Main Results:
- Phosphorylation dictates neurofilament and tau localization and assembly.
- Hyperphosphorylated tau aggregates in cell bodies in neurodegenerative diseases.
- Topographic regulation of phosphorylation is crucial for neuronal health.
Conclusions:
- Aberrant tau phosphorylation and aggregation are central to neurodegenerative disease progression.
- Understanding topographic regulation of phosphorylation offers therapeutic avenues for Alzheimer's disease.
- Filament systems are vital for cytoskeletal integrity and neuronal dynamics.
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