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Critical Roles of Deubiquitinating Enzymes in the Nervous System and Neurodegenerative Disorders

Post-translational modifications play major roles in the stability, function, and localization of target proteins involved in the nervous system. The ubiquitin-proteasome pathway uses small ubiquitin molecules to degrade neuronal proteins. Deubiquitinating enzymes (DUBs) reverse this degradation and...

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Autores principales: Das, Soumyadip, Ramakrishna, Suresh, Kim, Kye-Seong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Molecular and Cellular Biology 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103888/
https://www.ncbi.nlm.nih.gov/pubmed/32133826
http://dx.doi.org/10.14348/molcells.2020.2289
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author Das, Soumyadip
Ramakrishna, Suresh
Kim, Kye-Seong
author_facet Das, Soumyadip
Ramakrishna, Suresh
Kim, Kye-Seong
author_sort Das, Soumyadip
collection PubMed
description Post-translational modifications play major roles in the stability, function, and localization of target proteins involved in the nervous system. The ubiquitin-proteasome pathway uses small ubiquitin molecules to degrade neuronal proteins. Deubiquitinating enzymes (DUBs) reverse this degradation and thereby control neuronal cell fate, synaptic plasticity, axonal growth, and proper function of the nervous system. Moreover, mutations or downregulation of certain DUBs have been found in several neurodegenerative diseases, as well as gliomas and neuroblastomas. Based on emerging findings, DUBs represent an important target for therapeutic intervention in various neurological disorders. Here, we summarize advances in our understanding of the roles of DUBs related to neurobiology.
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spelling pubmed-71038882020-04-07 Critical Roles of Deubiquitinating Enzymes in the Nervous System and Neurodegenerative Disorders Das, Soumyadip Ramakrishna, Suresh Kim, Kye-Seong Mol Cells Minireview Post-translational modifications play major roles in the stability, function, and localization of target proteins involved in the nervous system. The ubiquitin-proteasome pathway uses small ubiquitin molecules to degrade neuronal proteins. Deubiquitinating enzymes (DUBs) reverse this degradation and thereby control neuronal cell fate, synaptic plasticity, axonal growth, and proper function of the nervous system. Moreover, mutations or downregulation of certain DUBs have been found in several neurodegenerative diseases, as well as gliomas and neuroblastomas. Based on emerging findings, DUBs represent an important target for therapeutic intervention in various neurological disorders. Here, we summarize advances in our understanding of the roles of DUBs related to neurobiology. Korean Society for Molecular and Cellular Biology 2020-03-31 2020-03-05 /pmc/articles/PMC7103888/ /pubmed/32133826 http://dx.doi.org/10.14348/molcells.2020.2289 Text en © The Korean Society for Molecular and Cellular Biology. All rights reserved. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/
spellingShingle Minireview
Das, Soumyadip
Ramakrishna, Suresh
Kim, Kye-Seong
Critical Roles of Deubiquitinating Enzymes in the Nervous System and Neurodegenerative Disorders
title Critical Roles of Deubiquitinating Enzymes in the Nervous System and Neurodegenerative Disorders
title_full Critical Roles of Deubiquitinating Enzymes in the Nervous System and Neurodegenerative Disorders
title_fullStr Critical Roles of Deubiquitinating Enzymes in the Nervous System and Neurodegenerative Disorders
title_full_unstemmed Critical Roles of Deubiquitinating Enzymes in the Nervous System and Neurodegenerative Disorders
title_short Critical Roles of Deubiquitinating Enzymes in the Nervous System and Neurodegenerative Disorders
title_sort critical roles of deubiquitinating enzymes in the nervous system and neurodegenerative disorders
topic Minireview
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103888/
https://www.ncbi.nlm.nih.gov/pubmed/32133826
http://dx.doi.org/10.14348/molcells.2020.2289
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