PKC-dependent phosphorylation of Munc18a at Ser313 in activated RBL-2H3 cells
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Protein Kinase C (PKC) regulates the release of pro-inflammatory compounds from IgE/antigen-activated mast cells by unknown mechanisms. In this study, we show for the first time that PKC inhibitor Ro-03-0432, which inhibits RBL-2H3 exocytosis/degranulation in a concentration-dependent fashion, prevents the phosphorylation of membrane fusion factor Munc18a at Ser 313. Our study provides fresh evidence that PKC-dependent protein phosphorylation may contribute to the intricate regulation of mast cell degranulation by directly targeting the fusion factors.
KeywordsProtein Kinase C Munc18a Mast cell degranulation RBL-2H3 Inflammation Phosphorylation
- 8.Parisotto D, Pfau M, Scheutzow A, Wild K, Mayer MP, Malsam J, Sinning I, Sollner TH. An extended helical conformation in domain 3a of Munc18-1 provides a template for SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex assembly. J Biol Chem. 2014;289:9639–50.CrossRefPubMedPubMedCentralGoogle Scholar