Cited by 143Neuroscience and Neuropharmacology ResearchProtein Kinase Regulation and GTPase SignalingSignaling Pathways in Disease

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Ca 2+ /calmodulin-dependent protein kinase II (CaMKII) is activated by calmodulin with two bound calciums

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Shifman, Julia M., Choi, Mee H., Mihalas, Stefan, Mayo, Stephen L., Kennedy, Mary B.·2006·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0606433103PMC PMC1599897

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Abstract

Changes in synaptic strength that underlie memory formation in the CNS are initiated by pulses of Ca2+ flowing through NMDA-type glutamate receptors into postsynaptic spines. Differences in the duration and size of the pulses determine whether a synapse is potentiated or depressed after repetitive synaptic activity. Calmodulin (CaM) is a major Ca2+ effector protein that binds up to four Ca2+ ions. CaM with bound Ca2+ can activate at least six signaling enzymes in the spine. In fluctuating cytosolic Ca2+, a large fraction of free CaM is bound to fewer than four Ca2+ ions. Binding to targets increases the affinity of CaM's remaining Ca2+-binding sites. Thus, initial binding of CaM to a target may depend on the target's affinity for CaM with only one or two bound Ca2+ ions. To study CaM-dependent signaling in the spine, we designed mutant CaMs that bind Ca2+ only at the two N-terminal or two C-terminal sites by using computationally designed mutations to stabilize the inactivated Ca2+-binding domains in the "closed" Ca2+-free conformation. We have measured their interactions with CaMKII, a major Ca2+/CaM target that mediates initiation of long-term potentiation. We show that CaM with two Ca2+ ions bound in its C-terminal lobe not only binds to CaMKII with low micromolar affinity but also partially activates kinase activity. Our results support the idea that competition for binding of CaM with two bound Ca2+ ions may influence significantly the outcome of local Ca2+ signaling in spines and, perhaps, in other signaling pathways.

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Authors: Shifman, J. M., Choi, M. H., Mihalas, S., Mayo, S. L., & Kennedy, M. B.
Affiliations: California Institute of Technology (US)
*Division of Biology and
ORCID: Shifman, Julia M.
Mayo, Stephen L.
Kennedy, Mary B.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2006-09-19
Volume: 103
Issue: 38
Pages: 13968-13973
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0606433103
PMC: PMC1599897
OpenAlex: W2020564163
Cited by: 143
References: 53
Citations by year: 2026: 6 · 2025: 5 · 2024: 1 · 2023: 10 · 2022: 6 · 2021: 6 · 2020: 5 · 2019: 9 · 2018: 8 · 2017: 6 · 2016: 6 · 2015: 6 · 2014: 7 · 2013: 6 · 2012: 11
FWCI: 3.67
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion)
Funders: Howard Hughes Medical Institute
Ralph M. Parsons Foundation
Rice University
U.S. Public Health Service
National Institute of Neurological Disorders and Stroke (NS 44306, NS047300, K25NS047300, P01NS044306)
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 › Signaling Pathways in Disease
Keywords: CaMKII, calmodulin, calcium binding sites, calmodulin mutants, kinase activation, synaptic plasticity, long-term potentiation, postsynaptic spines, computational protein design
MeSH terms: Calcium, Calmodulin, Computer Simulation, Enzyme Activation, Models, Molecular, Protein Binding, Protein Conformation, Synapses, Protein Folding, Calcium-Calmodulin-Dependent Protein Kinases, Calcium Signaling, Calcium-Calmodulin-Dependent Protein Kinase Type 2

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Ca 2+ /calmodulin-dependent protein kinase II (CaMKII) is activated by calmodulin with two bound calciums

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