Cargando…
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...
Autores principales: | , |
---|---|
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 |
_version_ | 1784581223070302208 |
---|---|
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. |
format | Online Article Text |
id | pubmed-8503901 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT sugimotochiho calmodulinacetylationamodificationtoremember AT robisonaj calmodulinacetylationamodificationtoremember |