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Protein kinase C and beyond

Nature Immunology volume 5, pages 785–790 (2004)Cite this article

Abstract

Protein kinase C molecules regulate both positive and negative signal transduction pathways essential for the initiation and homeostasis of immune responses. There are multiple isoforms of protein kinase C that are activated differently by calcium and diacylglycerol, and these are activated mainly by antigen receptors in T cells, B cells and mast cells. Additionally, mammals express several other diacylglycerol binding proteins that are linked to a network of key signal transduction pathways that control lymphocyte biology. Diacylglycerol and protein kinase C regulate a broad range of gene transcription programs but also modulate integrins, chemokine responses and antigen receptors, thereby regulating lymphocyte adhesion, migration, differentiation and proliferation.

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Figure 1: Classification and structural characteristics of PKC isoforms.
Figure 2: The network of DAG-binding proteins.
Figure 3: Activation of classical and novel PKC isoforms.

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Acknowledgements

We thank A. Altman, G. Baier and D. Littman and current and past members of the Lymphocyte Activation Laboratory for discussions. Supported by European Union Marie Curie (MCFI-2001-01855 to M.S.) and Wellcome Trust (D.C.).

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  1. Division of Cell Biology & Immunology, School of Life Sciences, University of Dundee, MSI/WTB Complex, Dow Street, Dundee, DD1 5EH, UK

    Martin Spitaler & Doreen A Cantrell

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Spitaler, M., Cantrell, D. Protein kinase C and beyond. Nat Immunol 5, 785–790 (2004). https://doi.org/10.1038/ni1097

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