Autophosphorylation of Ca2+/calmodulin-dependent protein kinase II. Effects on total and Ca2+-independent activities and kinetic parameters.
Open accessAbstract
Incubation of purified rat brain Ca2+/calmodulin-dependent protein kinase II for 2 min in the presence of Ca2+, calmodulin (CaM), Mg2+, and ATP converted the kinase from a completely Ca2+-dependent kinase to a substantially Ca2+-independent form with little loss of total activity. Subsequent addition of EGTA to the autophosphorylation reaction enhanced further autophosphorylation of the kinase which was associated with a suppression of total kinase activity to the Ca2+-independent value. Protein phosphatase 1 rapidly increased the suppressed total activity back to the control value and slowly decreased the Ca2+-independent activity. Kinetic analysis showed that the kinase not previously autophosphorylated had a Km for the synthetic peptide syntide-2 of 7 microM and Vmax of 9.8 mumol/min/mg when assayed in the presence of Ca2+ and CaM. The partially Ca2+-independent species, assayed in the presence of EGTA, had a Km of 21 microM and Vmax of 6.0. In the presence of Ca2+ and CaM the Km decreased and the Vmax increased to approximately control nonphosphorylated values. The completely Ca2+-independent form generated by sequential autophosphorylation first in the presence of Ca2+ and then EGTA had similar kinetic parameters to the partially independent species when assayed in the presence of EGTA, but addition of Ca2+ and CaM (up to 1 mg/ml) had little effect. These results suggest that separate autophosphorylation sites in the Ca2+/CaM-dependent protein kinase II are associated wi…
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Once Ca2+/CaM dissociates from a T286-phosphorylated kinase, autonomous activity phosphorylates T305 and T306, blocking Ca2+/CaM rebinding and braking further stimulation.
“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 [84]
T305/T306 phosphorylation does not directly inhibit kinase activity.
“However, it is important to note that T305/T306 phosphorylation does not directly inhibit kinase activity (84, 86).”
From Synaptic memory and CaMKII (2023) · cites this paper as [84]
Cites
Lai, Y., Nairn, A. C., & Greengard, P. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.12.4253 · Cited by 292 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Inhibitory Autophosphorylation of CaMKII Controls PSD Association, Plasticity, and Learning
Elgersma, Y., Fedorov, N. B., Ikonen, S., Choi, E. S., Elgersma, M., Carvalho, O. M., Giese, K. P., & Silva, A. J. (2002) · Neuron · doi:10.1016/s0896-6273(02)01007-3 · Cited by 290 · see citing works
Rellos, P., Pike, A. C. W., Niesen, F. H., Salah, E., Lee, W. H., von Delft, F., & Knapp, S. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000426 · Cited by 279 · see citing works
Patton, B. L., Miller, S. G., & Kennedy, M. B. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38577-1 · Cited by 165 · see citing works
Nicoll, R. A., & Schulman, H. (2023) · Physiological Reviews · doi:10.1152/physrev.00034.2022 · Cited by 126 · see citing works
- Authors
- Hashimoto, Y., Schworer, C. M., Colbran, R. J., & Soderling, T. R.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1987-06
- Volume
- 262
- Issue
- 17
- Pages
- 8051-8055
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1560918162
- Cited by
- 170
- References
- 1
- Citations by year
- 2025: 2 · 2024: 1 · 2023: 3 · 2021: 1 · 2020: 3 · 2019: 3 · 2018: 1 · 2017: 2 · 2016: 3 · 2014: 6 · 2013: 1 · 2012: 1
- FWCI
- 5.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Keywords
- calcium/calmodulin-dependent protein kinase II, autophosphorylation, calmodulin, protein phosphatase 1, enzyme kinetics, autophosphorylation sites, EGTA, ATP, rat brain
- MeSH terms
- Animals, Brain, Calcium, Egtazic Acid, Kinetics, Phosphorylation, Protein Kinases, Rats
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
