Cited by 292Protein Kinase Regulation and GTPase SignalingSignaling Pathways in DiseaseNeuroscience and Neuropharmacology Research

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Autophosphorylation reversibly regulates the Ca2+/calmodulin-dependence of Ca2+/calmodulin-dependent protein kinase II.

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Lai, Y, Nairn, A C, Greengard, P·1986·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.83.12.4253PMC PMC323710

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Abstract

Ca2+/calmodulin-dependent protein kinase II contains two subunits, alpha (Mr 50,000) and beta (Mr 60,000/58,000), both of which undergo Ca2+/calmodulin-dependent autophosphorylation. In the present study, we have studied the mechanism of this autophosphorylation reaction and its effect on the activity of the enzyme. Both subunits are autophosphorylated through an intramolecular mechanism. Using synapsin I as substrate, Ca2+/calmodulin-dependent protein kinase II, in its unphosphorylated form, was totally dependent on Ca2+ and calmodulin for its activity. Preincubation of the enzyme with Ca2+, calmodulin, and ATP, under conditions where autophosphorylation of both subunits occurred, converted the enzyme to one that was only partially dependent on Ca2+ and calmodulin for its activity. No change in the total activity, measured in the presence of Ca2+ and calmodulin, was observed. The nonhydrolyzable ATP analog adenosine 5'-[beta, gamma-imido] triphosphate did not substitute for ATP in the preincubation. Moreover, dephosphorylation of autophosphorylated Ca2+/calmodulin-dependent protein kinase II with protein phosphatase 2A resulted in an enzyme that was again totally dependent on Ca2+ and calmodulin for its activity. We propose that autophosphorylation and dephosphorylation reversibly regulate the Ca2+ and calmodulin requirement of Ca2+/calmodulin-dependent protein kinase II.

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Authors: Lai, Y., Nairn, A. C., & Greengard, P.
Affiliations: Rockefeller University (US)
ORCID: Nairn, A C
Greengard, P
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1986-06
Volume: 83
Issue: 12
Pages: 4253-4257
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.83.12.4253
PMC: PMC323710
OpenAlex: W2011962611
Cited by: 292
References: 33
Citations by year: 2026: 1 · 2025: 5 · 2023: 4 · 2022: 2 · 2021: 4 · 2020: 4 · 2019: 5 · 2018: 1 · 2017: 2 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 5 · 2012: 6
FWCI: 10.93
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)
Topics: 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
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords: calcium/calmodulin-dependent protein kinase II, autophosphorylation, kinase regulation, synapsin I, protein phosphatase 2A, dephosphorylation, ATP requirement, enzyme activation
MeSH terms: Adenosine Triphosphate, Animals, Calcium, Calmodulin, Enzyme Activation, Hot Temperature, Kinetics, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Structure-Activity Relationship, Rats, Protein Phosphatase 2

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Autophosphorylation reversibly regulates the Ca2+/calmodulin-dependence of Ca2+/calmodulin-dependent protein kinase II.

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