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Inflammation Research

, Volume 67, Issue 1, pp 1–3 | Cite as

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

  • Pratikshya Adhikari
  • Hao Xu
Short Communication

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

Protein Kinase C Munc18a Mast cell degranulation RBL-2H3 Inflammation Phosphorylation 

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Copyright information

© Springer International Publishing AG 2017

Authors and Affiliations

  1. 1.Department of Biological SciencesUniversity of Southern MississippiHattiesburgUSA

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