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.
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Items 201–212 of 212
Atypical protein kinase C in glucose metabolism
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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
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