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Calmodulin acetylation: A modification to remember

The formation of new memories appears to require alterations in the shape and strength of synapses within the hippocampus, yet our knowledge of the molecular mechanisms underlying these changes remains incomplete. Zhang and colleagues provide new understanding of memory formation by uncovering the l...

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Detalles Bibliográficos
Autores principales: Sugimoto, Chiho, Robison, A.J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8503901/
https://www.ncbi.nlm.nih.gov/pubmed/34606826
http://dx.doi.org/10.1016/j.jbc.2021.101273
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author Sugimoto, Chiho
Robison, A.J.
author_facet Sugimoto, Chiho
Robison, A.J.
author_sort Sugimoto, Chiho
collection PubMed
description The formation of new memories appears to require alterations in the shape and strength of synapses within the hippocampus, yet our knowledge of the molecular mechanisms underlying these changes remains incomplete. Zhang and colleagues provide new understanding of memory formation by uncovering the lysine acetyltransferase SRC3 as the key driver of the novel posttranslational modification of calmodulin (CaM) acetylation, which regulates CaM's activity and subsequent activation of CaMKII. This new pathway is demonstrated to be both necessary and sufficient for CA3→CA1 synapse long-term potentiation (LTP) and fear memory formation, and this approach may act as a blueprint for future investigation of the role of acetylation of other proteins in neuronal functions.
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spelling pubmed-85039012021-10-18 Calmodulin acetylation: A modification to remember Sugimoto, Chiho Robison, A.J. J Biol Chem Editors' Pick Highlight The formation of new memories appears to require alterations in the shape and strength of synapses within the hippocampus, yet our knowledge of the molecular mechanisms underlying these changes remains incomplete. Zhang and colleagues provide new understanding of memory formation by uncovering the lysine acetyltransferase SRC3 as the key driver of the novel posttranslational modification of calmodulin (CaM) acetylation, which regulates CaM's activity and subsequent activation of CaMKII. This new pathway is demonstrated to be both necessary and sufficient for CA3→CA1 synapse long-term potentiation (LTP) and fear memory formation, and this approach may act as a blueprint for future investigation of the role of acetylation of other proteins in neuronal functions. American Society for Biochemistry and Molecular Biology 2021-10-02 /pmc/articles/PMC8503901/ /pubmed/34606826 http://dx.doi.org/10.1016/j.jbc.2021.101273 Text en © 2021 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Editors' Pick Highlight
Sugimoto, Chiho
Robison, A.J.
Calmodulin acetylation: A modification to remember
title Calmodulin acetylation: A modification to remember
title_full Calmodulin acetylation: A modification to remember
title_fullStr Calmodulin acetylation: A modification to remember
title_full_unstemmed Calmodulin acetylation: A modification to remember
title_short Calmodulin acetylation: A modification to remember
title_sort calmodulin acetylation: a modification to remember
topic Editors' Pick Highlight
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8503901/
https://www.ncbi.nlm.nih.gov/pubmed/34606826
http://dx.doi.org/10.1016/j.jbc.2021.101273
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