The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
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…
Overview
Integrity signals
Registry
Cites
Statistics
Verification
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?
In the citing paper
“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]
Citations
Cites
A simplification of the protein assay method of Lowry et al. which is more generally applicable
Peterson, G. L. (1977) · Analytical Biochemistry · doi:10.1016/0003-2697(77)90043-4 · Cited by 8,531
PROTEIN SERINE/THREONINE KINASES
Edelman, A. M., Blumenthal, D., & Krebs, E. G. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.003031 · Cited by 1,435
Miller, S. (1986) · Cell · doi:10.1016/0092-8674(86)90008-5 · Cited by 864
Self-citationRoskoski, R. J. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)99034-1 · Cited by 831
Regional distribution of type II Ca2+/calmodulin-dependent protein kinase in rat brain
Erondu, N., & Kennedy, M. (1985) · The Journal of Neuroscience · doi:10.1523/jneurosci.05-12-03270.1985 · Cited by 630
Self-citationWatterson, D. M., Harrelson, W. G., Keller, P. M., Sharief, F. S., & VANAMAN, T. C. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33231-3 · Cited by 514
Bennett, M. K., Erondu, N. E., & Kennedy, M. B. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44239-6 · Cited by 481
Self-citationUeda, T., & Greengard, P. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40170-0 · Cited by 407
Colbran, R. J., Schworer, C. M., Hashimoto, Y., Fong, Y. L., Rich, D. P., Smith, M. K., & Soderling, T. R. (1989) · Biochemical Journal · doi:10.1042/bj2580313 · Cited by 406
Conti, M. A., & Adelstein, R. S. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69586-4 · Cited by 390
Research works printed but not linked: 3
- Stull, 1986, 17, 113
- Hanley, 1988, Biochem. Biophys. Res. Commun., 152, 122, 10.1016/S0006-291X(88)80688-0 · DOI
- Patton, 1988, Soc. Neurosci. Abstr., 14, 107
Cited by
Sorted by citations
Sensitivity of CaM Kinase II to the Frequency of Ca 2+ Oscillations
De Koninck, P., & Schulman, H. (1998) · Science · doi:10.1126/science.279.5348.227 · Cited by 1,269
A Dynamic Pathway for Calcium-Independent Activation of CaMKII by Methionine Oxidation
Erickson, J. R., Joiner, M.-L. A., Guan, X., Kutschke, W., Yang, J., Oddis, C. V., Bartlett, R. K., Lowe, J. S., O'Donnell, S. E., Aykin-Burns, N., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.048 · Cited by 1,122
Sumi, M., Kiuchi, K., Ishikawa, T., Ishii, A., Hagiwara, M., Nagatsu, T., & Hidaka, H. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)92031-e · Cited by 511
Hanson, P. I., Meyer, T., Stryer, L., & Schulman, H. (1994) · Neuron · doi:10.1016/0896-6273(94)90306-9 · Cited by 500
Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
Keranen, L. M., Sonnenburg, E. D., & Newton, A. C. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00277-6 · Cited by 470
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
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
