PKC-dependent phosphorylation of Munc18a at Ser313 in activated RBL-2H3 cells

Inflamm Res. 2018 Jan;67(1):1-3. doi: 10.1007/s00011-017-1097-4. Epub 2017 Oct 5.

Abstract

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.

Keywords: Inflammation; Mast cell degranulation; Munc18a; Phosphorylation; Protein Kinase C; RBL-2H3.

MeSH terms

  • Animals
  • Cell Degranulation
  • Cell Line, Tumor
  • Indoles / pharmacology
  • Mast Cells / physiology
  • Munc18 Proteins / metabolism*
  • Phosphorylation
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism*
  • Pyrroles / pharmacology
  • Rats

Substances

  • Indoles
  • Munc18 Proteins
  • Pyrroles
  • Ro 32-0432
  • Protein Kinase C