Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis

J Biol Chem. 2003 Sep 19;278(38):36410-7. doi: 10.1074/jbc.M306428200. Epub 2003 Jun 26.

Abstract

The p38 MAPK pathway regulates multiple neutrophil functional responses via activation of the serine-threonine kinase MAPK-activated protein kinase 2 (MAPKAPK2). To identify substrates of MAPKAPK2 that mediate these responses, a proteomic approach was used in which in vitro phosphorylation of neutrophil lysates by exogenously added active recombinant MAPKAPK2 was followed by protein separation using two-dimensional electrophoresis. Peptide mass fingerprinting of peptides defined by MALDI-MS was then utilized to identify phosphorylated proteins detected by autoradiography. Six candidate substrates were identified, including the p16 subunit of the seven-member Arp2/3 complex (p16-Arc). In vitro studies confirmed that MAPKAPK2 interacts with and phosphorylates the A isoform, but not the B isoform, of p16-Arc with a stoichiometry of 0.6 to 0.7. MAPKAPK2 also phosphorylated p16-Arc in intact Arp2/3 complexes precipitated from neutrophil lysates. Mutation of serine-77 to alanine on the A isoform prevented phosphorylation by MAPKAPK2. The ability of MAPKAPK2 to phosphorylate one isoform of p16-Arc suggests a possible mechanism by which the p38 MAPK cascade regulates remodeling of the actin cytoskeleton.

Publication types

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

MeSH terms

  • Actin-Related Protein 2
  • Actin-Related Protein 3
  • Actins / metabolism
  • Amino Acid Sequence
  • Cytoskeletal Proteins / chemistry*
  • Cytoskeleton / metabolism
  • Electrophoresis, Gel, Two-Dimensional
  • Glutathione Transferase / metabolism
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Mass Spectrometry
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / metabolism*
  • Mitogen-Activated Protein Kinases / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Neutrophils / chemistry
  • Neutrophils / enzymology*
  • Neutrophils / metabolism
  • Phosphorylation
  • Protein Binding
  • Protein Conformation
  • Protein Isoforms
  • Protein Serine-Threonine Kinases / chemistry*
  • Protein Serine-Threonine Kinases / metabolism
  • Protein Structure, Tertiary
  • Serine / chemistry
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Substrate Specificity
  • Trypsin / pharmacology
  • p38 Mitogen-Activated Protein Kinases

Substances

  • ACTR2 protein, human
  • ACTR3 protein, human
  • Actin-Related Protein 2
  • Actin-Related Protein 3
  • Actins
  • Cytoskeletal Proteins
  • Intracellular Signaling Peptides and Proteins
  • Microfilament Proteins
  • Protein Isoforms
  • Serine
  • Glutathione Transferase
  • MAP-kinase-activated kinase 2
  • Protein Serine-Threonine Kinases
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases
  • Trypsin