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Role of proteasome-dependent protein degradation in long-term operant memory in Aplysia

We investigated the in vivo role of protein degradation during intermediate (ITM) and long-term memory (LTM) in Aplysia using an operant learning paradigm. The proteasome inhibitor MG-132 inhibited the induction and molecular consolidation of LTM with no effect on ITM. Remarkably, maintenance of ste...

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Autores principales: Lyons, Lisa C., Gardner, Jacob S., Gandour, Catherine E., Krishnan, Harini C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5159658/
https://www.ncbi.nlm.nih.gov/pubmed/27980077
http://dx.doi.org/10.1101/lm.043794.116
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author Lyons, Lisa C.
Gardner, Jacob S.
Gandour, Catherine E.
Krishnan, Harini C.
author_facet Lyons, Lisa C.
Gardner, Jacob S.
Gandour, Catherine E.
Krishnan, Harini C.
author_sort Lyons, Lisa C.
collection PubMed
description We investigated the in vivo role of protein degradation during intermediate (ITM) and long-term memory (LTM) in Aplysia using an operant learning paradigm. The proteasome inhibitor MG-132 inhibited the induction and molecular consolidation of LTM with no effect on ITM. Remarkably, maintenance of steady-state protein levels through inhibition of protein synthesis using either anisomycin or rapamycin in conjunction with proteasome inhibition permitted the formation of robust 24 h LTM. Our studies suggest a primary role for proteasomal activity in facilitation of gene transcription for LTM and raise the possibility that synaptic mechanisms are sufficient to sustain 24 h memory.
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spelling pubmed-51596582018-01-01 Role of proteasome-dependent protein degradation in long-term operant memory in Aplysia Lyons, Lisa C. Gardner, Jacob S. Gandour, Catherine E. Krishnan, Harini C. Learn Mem Brief Communication We investigated the in vivo role of protein degradation during intermediate (ITM) and long-term memory (LTM) in Aplysia using an operant learning paradigm. The proteasome inhibitor MG-132 inhibited the induction and molecular consolidation of LTM with no effect on ITM. Remarkably, maintenance of steady-state protein levels through inhibition of protein synthesis using either anisomycin or rapamycin in conjunction with proteasome inhibition permitted the formation of robust 24 h LTM. Our studies suggest a primary role for proteasomal activity in facilitation of gene transcription for LTM and raise the possibility that synaptic mechanisms are sufficient to sustain 24 h memory. Cold Spring Harbor Laboratory Press 2017-01 /pmc/articles/PMC5159658/ /pubmed/27980077 http://dx.doi.org/10.1101/lm.043794.116 Text en © 2016 Lyons et al.; Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first 12 months after the full-issue publication date (see http://learnmem.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.
spellingShingle Brief Communication
Lyons, Lisa C.
Gardner, Jacob S.
Gandour, Catherine E.
Krishnan, Harini C.
Role of proteasome-dependent protein degradation in long-term operant memory in Aplysia
title Role of proteasome-dependent protein degradation in long-term operant memory in Aplysia
title_full Role of proteasome-dependent protein degradation in long-term operant memory in Aplysia
title_fullStr Role of proteasome-dependent protein degradation in long-term operant memory in Aplysia
title_full_unstemmed Role of proteasome-dependent protein degradation in long-term operant memory in Aplysia
title_short Role of proteasome-dependent protein degradation in long-term operant memory in Aplysia
title_sort role of proteasome-dependent protein degradation in long-term operant memory in aplysia
topic Brief Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5159658/
https://www.ncbi.nlm.nih.gov/pubmed/27980077
http://dx.doi.org/10.1101/lm.043794.116
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