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Cited by 49Neuroscience and Neuropharmacology ResearchProtein Kinase Regulation and GTPase SignalingProtein Structure and Dynamics

Assemblies of calcium/calmodulin-dependent kinase II with actin and their dynamic regulation by calmodulin in dendritic spines

Open access
Wang, Qian, Chen, Mingchen, Schafer, Nicholas P., Bueno, Carlos, Song, Sarah S., Hudmon, Andy, Wolynes, Peter G., Waxham, M. Neal +1 more·2019·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.1911452116PMC PMC6754556
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Abstract

Significance: The structural dynamics of the dendritic synapse, arising from the remodeling of actin cytoskeletons, has been widely associated with memory and cognition. The remodeling is regulated by intracellular Ca 2+ levels. Under low Ca 2+ concentration, actin filaments are bundled by a calcium signaling protein, CaMKII. When the Ca 2+ concentration is raised, CaMKII dissociates from actin and opens the window for actin remodeling. At present, the molecular details of the actin bundling and regulation are elusive. Herein we use experimental tools along with molecular simulations to construct a model of how CaMKII bundles actin and how the CaMKII–actin architecture is regulated by Ca 2+ signals. In this way, our results explain how Ca 2+ signals ultimately change the structure of the dendritic synapse.

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Crossref · 10.1073/pnas.1911452116

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  • Inactive CaMKIIβ, but not α, binds with high affinity to F-actin.

    “A second difference is the specific high-affinity binding of the inactive β, but not α, to F-actin (167–170).”

    From Synaptic memory and CaMKII (2023) · cites this paper as [170]

    The Discussion (page unavailable) says CaMKIIβ binds F-actin more strongly than CaMKIIα, but describes α as having a weaker interaction—not no interaction. The Results (page unavailable) also show that Ca2+/calmodulin promotes dissociation of the β–actin complex, consistent with binding in the inactive state. The categorical 'but not α' overstates the source. (LLM, conf=0.88)

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Cites

Flagged first, then by citations

Research works printed but not linked: 21

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Cited by

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Authors
Wang, Q., Chen, M., Schafer, N. P., Bueno, C., Song, S. S., Hudmon, A., Wolynes, P. G., Waxham, M. N., & Cheung, M. S.
Affiliations
  • Center for Theoretical Biological Physics (US)
  • The University of Texas Health Science Center at Houston (US)
  • Purdue University West Lafayette (US)
Corresponding author
  • Wolynes, Peter G.
  • Waxham, M. Neal
  • Cheung, Margaret S.
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2019-08-27
Volume
116
Issue
38
Pages
18937-18942
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.1911452116
PMC
PMC6754556
OpenAlex
W2970742362
Cited by
49
References
5
Citations by year
2026: 3 · 2025: 6 · 2024: 11 · 2023: 4 · 2022: 9 · 2021: 4 · 2020: 12
FWCI
2.99
Type
journal article
Language
en
Open access
Licence
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • Rice Research Repository (Rice University) (submittedVersion, cc-by-nc-nd)
Funders
  • NSF (PHY-1427654, CHE 1614101, CHE 1743392)
  • D.R. Bullard-Welch Chair at Rice University (Grant C-0016)
  • William Wheless III Professorship at UTHSC-Houston (Endowment)
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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
CaMKII, calmodulin, F-actin, dendritic spines, binding interface, regulatory domain, calcium signaling, actin filament remodeling, structural dynamics
MeSH terms
Protein Domains, Actins, Calcium, Calmodulin, Computer Simulation, Actin Cytoskeleton, Models, Molecular, Protein Binding, Dendritic Spines, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Protein Multimerization

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