PT  - JOURNAL ARTICLE
AU  - Adrienne S. Gordon
AU  - Lina Yao
AU  - Zhi-Liang Wu
AU  - Imogen R. Coe
AU  - Ivan Diamond
TI  - Ethanol Alters the Subcellular Localization of δ- and ε Protein Kinase C in NG108–15 Cells
AID  - 10.1124/mol.52.4.554
DP  - 1997 Oct 01
TA  - Molecular Pharmacology
PG  - 554--559
VI  - 52
IP  - 4
4099  - http://molpharm.aspetjournals.org/content/52/4/554.short
4100  - http://molpharm.aspetjournals.org/content/52/4/554.full
SO  - Mol Pharmacol1997 Oct 01; 52
AB  - Protein kinase C (PKC) has been shown to regulate the ethanol sensitivity of membrane-bound receptors and transporters, but little is known about the molecular mechanisms underlying this regulation. PKC is a family of isozymes that translocate to new intracellular sites on activation. Here we present immunochemical data showing that ethanol causes translocation of δ- and ε-PKC to new intracellular sites. Ethanol causes translocation of δ-PKC from the Golgi to the perinucleus; this translocation is similar to that induced by activation of PKC with phorbol esters. In contrast, ε-PKC translocation caused by ethanol is different from that induced by phorbol esters; ethanol causes translocation of ε-PKC from the perinucleus to the cytoplasm, whereas phorbol ester activation causes translocation of ε-PKC to the nucleus. Because the substrate specificity of these kinases is determined by their site of localization, ethanol-induced translocation of δ- and ε-PKC to new intracellular sites may explain some of the pleiotropic effects of ethanol on cellular functions.