Kinase MPK17 and the Peroxisome Division Factor PMD1 Influence Salt-induced Peroxisome Proliferation

Plant Physiol. 2018 Jan;176(1):340-351. doi: 10.1104/pp.17.01019. Epub 2017 Sep 20.

Abstract

Peroxisomes are small organelles that house many oxidative reactions. Peroxisome proliferation is induced under multiple stress conditions, including salt stress; however, factors regulating this process are not well defined. We have identified a role for Arabidopsis (Arabidopsis thaliana) MAP KINASE17 (MPK17) in affecting peroxisome division in a manner that requires the known peroxisome division factor PEROXISOME AND MITOCHONDRIAL DIVISION FACTOR1 (PMD1). MPK17 and PMD1 are involved in peroxisome proliferation in response to NaCl stress. Additionally, we found that PMD1 is an actin-binding protein and that a functioning actin cytoskeleton is required for NaCl-induced peroxisome division. Our data suggest roles for MPK17 and PMD1 in influencing the numbers and cellular distribution of peroxisomes through the cytoskeleton-peroxisome connection. These findings expand our understanding of peroxisome division and potentially identify factors connecting the actin cytoskeleton and peroxisome proliferation.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actins / metabolism
  • Arabidopsis / drug effects
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / metabolism*
  • Indoleacetic Acids / pharmacology
  • Membrane Proteins / metabolism*
  • Mitogen-Activated Protein Kinases / metabolism*
  • Models, Biological
  • Mutation / genetics
  • Peroxisomes / drug effects
  • Peroxisomes / metabolism*
  • Phenotype
  • Polymerization
  • Protein Binding / drug effects
  • Sodium Chloride / pharmacology*

Substances

  • Actins
  • Arabidopsis Proteins
  • Indoleacetic Acids
  • Membrane Proteins
  • PMD1 protein, Arabidopsis
  • Sodium Chloride
  • MPK17 protein, Arabidopsis
  • Mitogen-Activated Protein Kinases