An Evolutionarily Conserved PLC-PKD-TFEB Pathway for Host Defense

Cell Rep. 2016 May 24;15(8):1728-42. doi: 10.1016/j.celrep.2016.04.052. Epub 2016 May 12.

Abstract

The mechanisms that tightly control the transcription of host defense genes have not been fully elucidated. We previously identified TFEB as a transcription factor important for host defense, but the mechanisms that regulate TFEB during infection remained unknown. Here, we used C. elegans to discover a pathway that activates TFEB during infection. Gene dkf-1, which encodes a homolog of protein kinase D (PKD), was required for TFEB activation in nematodes infected with Staphylococcus aureus. Conversely, pharmacological activation of PKD was sufficient to activate TFEB. Furthermore, phospholipase C (PLC) gene plc-1 was also required for TFEB activation, downstream of Gαq homolog egl-30 and upstream of dkf-1. Using reverse and chemical genetics, we discovered a similar PLC-PKD-TFEB axis in Salmonella-infected mouse macrophages. In addition, PKCα was required in macrophages. These observations reveal a previously unknown host defense signaling pathway, which has been conserved across one billion years of evolution.

MeSH terms

  • Animals
  • Basic Helix-Loop-Helix Leucine Zipper Transcription Factors / metabolism*
  • Caenorhabditis elegans / microbiology*
  • Caenorhabditis elegans Proteins / metabolism
  • Enzyme Activation
  • Evolution, Molecular*
  • Host-Pathogen Interactions / immunology*
  • Macrophages / metabolism
  • Macrophages / microbiology
  • Mice
  • Microbial Viability
  • Protein Kinase C / metabolism*
  • Protein Kinase C-alpha / metabolism
  • RAW 264.7 Cells
  • Salmonella enterica / physiology
  • Signal Transduction*
  • Staphylococcal Infections / enzymology
  • Staphylococcal Infections / microbiology
  • Staphylococcal Infections / pathology
  • Staphylococcus aureus / physiology
  • Type C Phospholipases / metabolism*

Substances

  • Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
  • Caenorhabditis elegans Proteins
  • protein kinase D
  • Protein Kinase C
  • Protein Kinase C-alpha
  • Type C Phospholipases