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Activation of type II calcium/calmodulin-dependent protein kinase by Ca2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain.
Open accessAbstract
It is now well established that autophosphorylation of a threonine residue located next to each calmodulin-binding domain in the subunits of type II Ca2+/calmodulin-dependent protein kinase causes the kinase to remain active, although at a reduced rate, after Ca2+ is removed from the reaction. This autophosphorylated form of the kinase is still sensitive to Ca2+/calmodulin, which is required for a maximum catalytic rate. After removal of Ca2+, new sites are autophosphorylated by the partially active kinase. Autophosphorylation of these sites abolishes sensitivity of the kinase to Ca2+/calmodulin (Hashimoto, Y., Schworer, C. M., Colbran, R. J., and Soderling, T. R. (1987) J. Biol. Chem. 262, 8051-8055). We have identified two pairs of homologous residues, Thr305 and Ser314 in the alpha subunit and Thr306 and Ser315 in the beta subunit, that are autophosphorylated only after removal of Ca2+ from an autophosphorylation reaction. The sites were identified by direct sequencing of labeled tryptic phosphopeptides isolated by reverse-phase high pressure liquid chromatography. Thr305-306 is rapidly dephosphorylated by purified protein phosphatases 1 and 2A, whereas Ser314-315 is resistant to dephosphorylation. We have shown by selective dephosphorylation that the presence of phosphate on Thr305-306 blocks sensitivity of the kinase to Ca2+/calmodulin. In contrast, the presence of phosphate on Ser314-315 is associated with an increase in the Kact for Ca2+/calmodulin of only about 2-fold…
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“However, once Ca2+/CaM dissociates from a kinase phosphorylated at T286, its autonomous activity quickly phosphorylates T305 and T306, blocking rebinding of Ca2+/CaM and exerting a brake on further Ca2+/CaM stimulation, in what is at times referred to as inhibitory autophosphorylation (80, 84–86).”
From Synaptic memory and CaMKII (2023) · cites this paper as [85]
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Metadata
- Authors
- Patton, B. L., Miller, S. G., & Kennedy, M. B.
- Affiliations
- California Institute of Technology (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-07
- Volume
- 265
- Issue
- 19
- Pages
- 11204-11212
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1505515840
- Cited by
- 165
- References
- 40
- Citations by year
- 2025: 1 · 2023: 3 · 2022: 4 · 2021: 7 · 2020: 7 · 2019: 3 · 2018: 4 · 2017: 4 · 2016: 1 · 2015: 2 · 2014: 3 · 2013: 4 · 2012: 4
- FWCI
- 4.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- National Institutes of Health (5t32ns007251-22)
- National Institute of Neurological Disorders and Stroke (R01NS017660, NS-17660, NS-07251)
- 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
- autophosphorylation, calmodulin-binding domain, threonine phosphorylation, serine phosphorylation, kinase activation, protein phosphatase 1, protein phosphatase 2A, dephosphorylation, alpha and beta subunits
- MeSH terms
- Adenosine Triphosphate, Amino Acid Sequence, Animals, Binding Sites, Calcium, Calmodulin, Cattle, Chromatography, High Pressure Liquid, Enzyme Activation, Kinetics, Molecular Sequence Data, Peptide Fragments, Phosphorylation, Phosphoserine, Phosphothreonine, Protein Kinases, Rabbits, Threonine, Trypsin, Calcium-Calmodulin-Dependent Protein Kinases, Rats
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