PKC-Dependent Phosphorylation of Munc18a at Ser313 in Activated RBL-2H3 Cells
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.
(2018). PKC-Dependent Phosphorylation of Munc18a at Ser313 in Activated RBL-2H3 Cells. Inflammation Research, 67(1), 1-3.
Available at: https://aquila.usm.edu/fac_pubs/15590