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CaMKII holoenzyme mechanisms that govern the LTP versus LTD decision

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Cook, Sarah G., Buonarati, Olivia R., Coultrap, Steven J., Bayer, K. Ulrich·2021·Science Advances
DOI 10.1126/sciadv.abe2300PMC PMC8046365
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Abstract

Molecular signal computation within the CaMKII holoenzyme determines the direction of synaptic plasticity.

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Crossref · 10.1126/sciadv.abe2300

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  • T305/T306 phosphorylation selectively promotes LTD.

    “Finally, another proposal also focuses on CaMKII and the phosphorylation of T305/T306, which selectively promotes LTD (402).”

    From Synaptic memory and CaMKII (2023) · cites this paper as [402]

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Authors
Cook, S. G., Buonarati, O. R., Coultrap, S. J., & Bayer, K. U.
Affiliations
University of Colorado Anschutz (US)
Corresponding author
Bayer, K. Ulrich
ORCID
Venue
Science Advances
Publisher
American Association for the Advancement of Science (AAAS)
Published
2021-04-16
Volume
7
Issue
16
ISSN
2375-2548 (ISSN-L)
DOI
10.1126/sciadv.abe2300
PMC
PMC8046365
OpenAlex
W3155432123
Cited by
74
References
5
Citations by year
2026: 13 · 2025: 13 · 2024: 10 · 2023: 12 · 2022: 17 · 2021: 9
FWCI
5.53
Type
journal article
Language
en
Open access
Licence
Locations
  • Science Advances (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institute on Aging (F31AG062160, F32AG066536, R01AG067713)
  • National Institute of General Medical Sciences (T32GM007635)
  • National Institute of Neurological Disorders and Stroke (P30NS048154, R01NS081248, R01NS110383)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
Keywords
long-term potentiation, long-term depression, feedforward inhibition, neuroplasticity, synaptic plasticity

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