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Local ubiquitin-proteasome-mediated proteolysis and long-term synaptic plasticity

The ubiquitin-proteasome pathway (UPP) of protein degradation has many roles in synaptic plasticity that underlies memory. Work on both invertebrate and vertebrate model systems has shown that the UPP regulates numerous substrates critical for synaptic plasticity. Initial research took a global view...

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Autores principales: Hegde, Ashok N., Haynes, Kathryn A., Bach, Svitlana V., Beckelman, Brenna C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4248836/
https://www.ncbi.nlm.nih.gov/pubmed/25520617
http://dx.doi.org/10.3389/fnmol.2014.00096
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author Hegde, Ashok N.
Haynes, Kathryn A.
Bach, Svitlana V.
Beckelman, Brenna C.
author_facet Hegde, Ashok N.
Haynes, Kathryn A.
Bach, Svitlana V.
Beckelman, Brenna C.
author_sort Hegde, Ashok N.
collection PubMed
description The ubiquitin-proteasome pathway (UPP) of protein degradation has many roles in synaptic plasticity that underlies memory. Work on both invertebrate and vertebrate model systems has shown that the UPP regulates numerous substrates critical for synaptic plasticity. Initial research took a global view of ubiquitin-protein degradation in neurons. Subsequently, the idea of local protein degradation was proposed a decade ago. In this review, we focus on the functions of the UPP in long-term synaptic plasticity and discuss the accumulated evidence in support of the idea that the components of the UPP often have disparate local roles in different neuronal compartments rather than a single cell-wide function.
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spelling pubmed-42488362014-12-17 Local ubiquitin-proteasome-mediated proteolysis and long-term synaptic plasticity Hegde, Ashok N. Haynes, Kathryn A. Bach, Svitlana V. Beckelman, Brenna C. Front Mol Neurosci Neuroscience The ubiquitin-proteasome pathway (UPP) of protein degradation has many roles in synaptic plasticity that underlies memory. Work on both invertebrate and vertebrate model systems has shown that the UPP regulates numerous substrates critical for synaptic plasticity. Initial research took a global view of ubiquitin-protein degradation in neurons. Subsequently, the idea of local protein degradation was proposed a decade ago. In this review, we focus on the functions of the UPP in long-term synaptic plasticity and discuss the accumulated evidence in support of the idea that the components of the UPP often have disparate local roles in different neuronal compartments rather than a single cell-wide function. Frontiers Media S.A. 2014-12-01 /pmc/articles/PMC4248836/ /pubmed/25520617 http://dx.doi.org/10.3389/fnmol.2014.00096 Text en Copyright © 2014 Hegde, Haynes, Bach and Beckelman. http://creativecommons.org/licenses/by/4.0/ 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
Hegde, Ashok N.
Haynes, Kathryn A.
Bach, Svitlana V.
Beckelman, Brenna C.
Local ubiquitin-proteasome-mediated proteolysis and long-term synaptic plasticity
title Local ubiquitin-proteasome-mediated proteolysis and long-term synaptic plasticity
title_full Local ubiquitin-proteasome-mediated proteolysis and long-term synaptic plasticity
title_fullStr Local ubiquitin-proteasome-mediated proteolysis and long-term synaptic plasticity
title_full_unstemmed Local ubiquitin-proteasome-mediated proteolysis and long-term synaptic plasticity
title_short Local ubiquitin-proteasome-mediated proteolysis and long-term synaptic plasticity
title_sort local ubiquitin-proteasome-mediated proteolysis and long-term synaptic plasticity
topic Neuroscience
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4248836/
https://www.ncbi.nlm.nih.gov/pubmed/25520617
http://dx.doi.org/10.3389/fnmol.2014.00096
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