The DOI matches its Crossref record; 212 of the 212 references it cites were found in a registry or an index.
Structural Basis of Protein Kinase C Isoform Function
Open accessAbstract
Protein kinase C (PKC) isoforms comprise a family of lipid-activated enzymes that have been implicated in a wide range of cellular functions. PKCs are modular enzymes comprised of a regulatory domain (that contains the membrane-targeting motifs that respond to lipid cofactors, and in the case of some PKCs calcium) and a relatively conserved catalytic domain that binds ATP and substrates. These enzymes are coexpressed and respond to similar stimulatory agonists in many cell types. However, there is growing evidence that individual PKC isoforms subserve unique (and in some cases opposing) functions in cells, at least in part as a result of isoform-specific subcellular compartmentalization patterns, protein-protein interactions, and posttranslational modifications that influence catalytic function. This review focuses on the structural basis for differences in lipid cofactor responsiveness for individual PKC isoforms, the regulatory phosphorylations that control the normal maturation, activation, signaling function, and downregulation of these enzymes, and the intra-/intermolecular interactions that control PKC isoform activation and subcellular targeting in cells. A detailed understanding of the unique molecular features that underlie isoform-specific posttranslational modification patterns, protein-protein interactions, and subcellular targeting (i.e., that impart functional specificity) should provide the basis for the design of novel PKC isoform-specific activator or inhibitor compounds that can achieve therapeutically useful changes in PKC signaling in cells.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Specificity and mechanism of action of some commonly used protein kinase inhibitors
DAVIES, S. P., REDDY, H., CAIVANO, M., & COHEN, P. (2000) · Biochemical Journal · doi:10.1042/bj3510095 · Cited by 3,132
Knighton, D. R., Zheng, J., Ten Eyck, L. F., Ashford, V. A., Xuong, N.-H., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862342 · Cited by 1,759
The multiple faces of caveolae
Parton, R. G., & Simons, K. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2122 · Cited by 1,454
Protein Kinase C Isotypes Controlled by Phosphoinositide 3-Kinase Through the Protein Kinase PDK1
Le Good, J. A., Ziegler, W. H., Parekh, D. B., Alessi, D. R., Cohen, P., & Parker, P. J. (1998) · Science · doi:10.1126/science.281.5385.2042 · Cited by 1,110
Protein kinase C and other diacylglycerol effectors in cancer
Griner, E. M., & Kazanietz, M. G. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2110 · Cited by 978
Knighton, D. R., Zheng, J., Ten Eyck, L. F., Xuong, N.-H., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862343 · Cited by 960
Protein kinase C isozymes and the regulation of diverse cell responses
Dempsey, E. C., Newton, A. C., Mochly-Rosen, D., Fields, A. P., Reyland, M. E., Insel, P. A., & Messing, R. O. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.3.l429 · Cited by 737
Activation of the T24 bladder carcinoma transforming gene is linked to a single amino acid change
Taparowsky, E., Suard, Y., Fasano, O., Shimizu, K., Goldfarb, M., & Wigler, M. (1982) · Nature · doi:10.1038/300762a0 · Cited by 703
Protein kinase C signaling and oxidative stress
Gopalakrishna, R., & Jaken, S. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00221-5 · Cited by 701 · cited 1×
“While the focus of most studies in the literature has been on the effects of oxidative stress to activate Src family kinases and alter PKC signaling mechanisms through PKC tyrosine phosphorylation, PKCs are also direct targets for redox modifications (69).”
BackgroundProteolytic activation of protein kinase C delta by an ICE-like protease in apoptotic cells.
Emoto, Y., Manome, Y., Meinhardt, G., Kisaki, H., Kharbanda, S., Robertson, M., Ghayur, T., Wong, W. W., Kamen, R., & Weichselbaum, R. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00305.x · Cited by 670
Cited by
Reactive Oxygen Species in Inflammation and Tissue Injury
Mittal, M., Siddiqui, M. R., Tran, K., Reddy, S. P., & Malik, A. B. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5149 · Cited by 4,897
Mechanisms of Insulin Action and Insulin Resistance
Petersen, M. C., & Shulman, G. I. (2018) · Physiological Reviews · doi:10.1152/physrev.00063.2017 · Cited by 3,028
Signaling in Muscle Contraction
Kuo, I. Y., & Ehrlich, B. E. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a006023 · Cited by 424
DAG tales: the multiple faces of diacylglycerol—stereochemistry, metabolism, and signaling
Eichmann, T. O., & Lass, A. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1982-3 · Cited by 314
Nishitsuji, K., Hosono, T., Nakamura, T., Bu, G., & Michikawa, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225532 · Cited by 275
Metadata
- Authors
- Steinberg, S. F.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2008-10
- Volume
- 88
- Issue
- 4
- Pages
- 1341-1378
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W1998349282
- Cited by
- 872
- References
- 212
- FWCI
- 2.36
- Type
- journal article
- Language
- en
- Open access
- green
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Structural Basis of Protein Kinase C Isoform Function. https://app.cochat.ai/papers/10.1152/physrev.00034.2007
- The paper
- Steinberg, S. F. (2008). Structural Basis of Protein Kinase C Isoform Function. Physiological Reviews. https://doi.org/10.1152/physrev.00034.2007
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
