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Cited by 91Protein Kinase Regulation and GTPase SignalingSignaling Pathways in DiseaseS100 Proteins and Annexins

Active site-directed inhibition of Ca2+/calmodulin-dependent protein kinase type II by a bifunctional calmodulin-binding peptide.

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Kelly, P T, Weinberger, R P, Waxham, M N·1988·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.85.14.4991PMC PMC281673
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Abstract

The activation of Ca2+/calmodulin (CaM)-dependent protein kinase II (CaM-KII) by Ca2+/CaM results in autophosphorylation and the generation of Ca2+/CaM-independent enzyme activity. We postulated that CaM binding and subsequent autophosphorylation alters the conformation of CaM-KII and exposes its substrate-binding and catalytic site(s). Previous peptide mapping studies on CaM-KII demonstrated the close proximity of CaM-binding and autophosphorylation domains. Analyses of the deduced amino acid sequences encoding CaM-KII have allowed the identification of its CaM-binding domain and have revealed two consensus phosphorylation sites that flank this regulatory domain. We report herein the distinct properties of two synthetic peptides modeled after the CaM-binding domain of CaM-KII. The first peptide binds CaM in a Ca2+-dependent manner and is an antagonist of CaM-KII activation (IC50 approximately equal to 75 nM). It does not, however, inhibit CaM-KII activity. A second peptide containing the same CaM-binding domain plus a putative autophosphorylation sequence at its N terminus displayed bifunctional regulatory properties. In addition to being a CaM antagonist, the latter was a potent inhibitor of Ca2+/CaM-independent kinase activity (IC50 approximately equal to 2 microM). We suggest that this bifunctional peptide represents an active site-directed inhibitory element of CaM-KII. The separation of CaM antagonist and active site-directed inhibitory properties of this peptide distinguishes CaM-KII from other CaM-dependent enzymes in which bifunctional regulatory properties appear to reside in the same peptide domain. These results indicate that the definition of site-directed inhibitory peptides should, in some cases, be expanded to include bona fide phosphorylation sites.

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Crossref · 10.1073/pnas.85.14.4991

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  • CaMKII contains an autoinhibitory regulatory segment that binds across the substrate binding groove.

    “As is the case with many kinases, CaMKII contains an autoinhibitory regulatory segment (FIGURE 2, A, B1, AND B2) that binds across the substrate binding groove, whose structure and function have been delineated by peptides, mutations, and crystallography (71–77).”

    From Synaptic memory and CaMKII (2023) · cites this paper as [77]

    The Abstract identifies a CaMKII regulatory domain and reports that a peptide modeled on it inhibits kinase activity; the authors suggest it acts as an active site-directed inhibitory element. The available passage does not establish that the regulatory segment binds across the substrate-binding groove, so that structural detail is not supported by this source. (LLM, conf=0.82)

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Authors
Kelly, P. T., Weinberger, R. P., & Waxham, M. N.
Affiliations
The University of Texas Health Science Center at Houston (US)
ORCID
Waxham, M N
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1988-07
Volume
85
Issue
14
Pages
4991-4995
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.85.14.4991
PMC
PMC281673
OpenAlex
W1970395634
Cited by
91
References
1
Citations by year
2023: 1 · 2022: 1 · 2021: 1 · 2018: 1 · 2015: 1 · 2012: 1
FWCI
5.28
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of Neurological Disorders and Stroke (NS-22452)
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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
Keywords
calcium/calmodulin-dependent protein kinase II, calmodulin-binding domain, active site-directed inhibition, bifunctional peptides, calmodulin antagonists, autophosphorylation, phosphorylation sites, kinase regulation, peptide mapping
MeSH terms
Amino Acid Sequence, Binding Sites, Calcium, Calmodulin, Enzyme Activation, Kinetics, Molecular Sequence Data, Nerve Tissue Proteins, Peptides, Phosphorylation, Synapsins, Protein Kinase Inhibitors

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

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