PKC-delta translocates to plasma membrane

Stable Identifier
Homo sapiens
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Protein kinase C-delta (PRKCD), activated upon CLEC7A (Dectin-1)-SYK signaling, phosphorylates CARD9 leading to NF-kB activation (Strasser et al. 2012) and complex formation between CARD9 and BCL10. CLEC6A (Dectin-2) and CLEC4E (Mincle) also induces intracellular signaling through PRKCD and CARD9-BCL10-MALT1 pathway. Similar to the CLEC7A responses, both CLEC6A and CLEC4E-induced interleukin 10 (IL10) and tumour necrotic factor (TNF) production were severely impaired in the absence of PRKCD (Strasser et al. 2012). PRKCD is a member of the Ca2+ independent and diacylglycerol (DAG) dependent novel PKC subfamily. PKC family members exist in an immature inactive conformation that requires post-translational modifications to achieve catalytic maturity. The catalytic maturation of PRKCD involves the auto-phosphorylation of Ser645 and the phosphorylation of Thr507 and Ser664 (Li et al. 1997, Keranen et al. 1995). These phosphorylations of activation loop residues act as a priming step that allows the catalytic maturation of PRKCD (Dutil et al. 1998). Fully phosphorylated and primed PRKCD localises to the cytosol with its pseudosubstrate occupying the substrate-binding cavity. Signals that cause the lipid hydrolysis recruit PKC to membranes. The C1 domain in PRKCD is a cysteine-rich compact structure, identified as the interaction site for DAG and phorbol ester. PRKCD preferentially translocates to the plasma membrane (Stahelin et al. 2004, Newton 2010).

Literature References
PubMed ID Title Journal Year
15105418 Mechanism of diacylglycerol-induced membrane targeting and activation of protein kinase Cdelta

Cho, W, Rafter, JD, Digman, MA, Medkova, M, Stahelin, RV, Melowic, HR, Ananthanarayanan, B

J. Biol. Chem. 2004
7499357 Protein kinase C: structure, function, and regulation

Newton, AC

J. Biol. Chem. 1995
12473183 Protein kinase C delta (PKC delta): activation mechanisms and functions

Matsuzaki, H, Yamamoto, T, Kikkawa, U

J. Biochem. 2002
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