Ca, cAMP & Lipid Signaling

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Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation at Thr500 in the activation loop, the autophosphorylation site at Thr641, and at carboxy-terminal hydrophobic site Ser660 occurs in vivo (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. Either the enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).

1. Nishizuka, Y. (1984) Nature 308, 693-698.
2. Keranen, L.M. et al. (1995) Curr. Biol. 5, 1394-1403.
3. Mellor, H. and Parker, P.J. (1998) Biochem J. 332 (Pt 2), 281-292.
4. Ron, D. and Kazanietz, M.G. (1999) FASEB J. 13, 1658-1676.
5. Moscat, J. and Diaz-Meco, M.T. (2000) EMBO Rep. 1, 399-403.
6. Baron, C.L. and Malhotra, V. (2002) Science 295, 325-328.
7. Flynn, P. et al. (2000) J. Biol. Chem. 275, 11064-11070.

• Deszo, E. L. et al. (2001) Cd45 negatively regulates monocytic cell differentiation by inhibiting phorbol 12-myristate13-acetate-dependent activation and tyrosine phosphorylation of protein kinase c delta. J. Biol. Chem. 276, 10212-10217. Applications: Western Blotting
• Sweeney, C. et al. (2001) Growth Factor-specific Signaling Pathway Stimulation and Gene Expression Mediated by ErbB Receptors. J. Biol. Chem. 276, 22685-22698. Applications: Western Blotting
• Iwabu, A. et al. (2004) Epidermal growth factor induces fibroblast contractility and motility via a protein kinase C delta-dependent pathway. J. Biol. Chem. 279, 14551-14560. Applications: Western Blotting
• Godbout, J. P. et al. (2002) Methylglyoxal Enhances Cisplatin-induced Cytotoxicity by Activating Protein Kinase C-delta. J. Biol. Chem 277 (4), 2554-2561. Applications: Western Blotting
• Leinweber, B. et al. (2000) Regulation of protein kinase C by the cytoskeletal protein calponin. J. Biol. Chem. 275, 40329-40336. Applications: Western Blotting

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Phospho-PKC (pan) (βII Ser660) Antibody

©1999-2012 Cell Signaling Technology, Inc.

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