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Ubiquitin pathways in neurodegenerative disease

Control of proper protein synthesis, function, and turnover is essential for the health of all cells. In neurons these demands take on the additional importance of supporting and regulating the highly dynamic connections between neurons that are necessary for cognitive function, learning, and memory...

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Detalles Bibliográficos
Autores principales: Atkin, Graham, Paulson, Henry
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4085722/
https://www.ncbi.nlm.nih.gov/pubmed/25071440
http://dx.doi.org/10.3389/fnmol.2014.00063
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author Atkin, Graham
Paulson, Henry
author_facet Atkin, Graham
Paulson, Henry
author_sort Atkin, Graham
collection PubMed
description Control of proper protein synthesis, function, and turnover is essential for the health of all cells. In neurons these demands take on the additional importance of supporting and regulating the highly dynamic connections between neurons that are necessary for cognitive function, learning, and memory. Regulating multiple unique synaptic protein environments within a single neuron while maintaining cell health requires the highly regulated processes of ubiquitination and degradation of ubiquitinated proteins through the proteasome. In this review, we examine the effects of dysregulated ubiquitination and protein clearance on the handling of disease-associated proteins and neuronal health in the most common neurodegenerative diseases.
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spelling pubmed-40857222014-07-28 Ubiquitin pathways in neurodegenerative disease Atkin, Graham Paulson, Henry Front Mol Neurosci Neuroscience Control of proper protein synthesis, function, and turnover is essential for the health of all cells. In neurons these demands take on the additional importance of supporting and regulating the highly dynamic connections between neurons that are necessary for cognitive function, learning, and memory. Regulating multiple unique synaptic protein environments within a single neuron while maintaining cell health requires the highly regulated processes of ubiquitination and degradation of ubiquitinated proteins through the proteasome. In this review, we examine the effects of dysregulated ubiquitination and protein clearance on the handling of disease-associated proteins and neuronal health in the most common neurodegenerative diseases. Frontiers Media S.A. 2014-07-08 /pmc/articles/PMC4085722/ /pubmed/25071440 http://dx.doi.org/10.3389/fnmol.2014.00063 Text en Copyright © 2014 Atkin and Paulson. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Neuroscience
Atkin, Graham
Paulson, Henry
Ubiquitin pathways in neurodegenerative disease
title Ubiquitin pathways in neurodegenerative disease
title_full Ubiquitin pathways in neurodegenerative disease
title_fullStr Ubiquitin pathways in neurodegenerative disease
title_full_unstemmed Ubiquitin pathways in neurodegenerative disease
title_short Ubiquitin pathways in neurodegenerative disease
title_sort ubiquitin pathways in neurodegenerative disease
topic Neuroscience
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4085722/
https://www.ncbi.nlm.nih.gov/pubmed/25071440
http://dx.doi.org/10.3389/fnmol.2014.00063
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