Merlin phosphorylation by p21-activated kinase 2 and effects of phosphorylation on merlin localization.

Academic Article

Abstract

  • The Nf2 tumor suppressor gene product merlin is related to the membrane-cytoskeleton linker proteins of the band 4.1 superfamily, including ezrin, radixin, and moesin (ERMs). Merlin is regulated by phosphorylation in a Rac/cdc42-dependent fashion. We report that the phosphorylation of merlin at serine 518 is induced by the p21-activated kinase PAK2. This is demonstrated by biochemical fractionation, use of active and dominant-negative mutants of PAK2, and immunodepletion. By using wild-type and mutated forms of merlin and phospho-directed antibodies, we show that phosphorylation of merlin at serine 518 leads to dramatic protein relocalization.
  • Authors

  • Kissil, Joseph L
  • Johnson, Kristen
  • Eckman, Matthew S
  • Jacks, Tyler
  • Status

    Publication Date

  • March 22, 2002
  • Published In

    Keywords

  • 3T3 Cells
  • Animals
  • Blotting, Western
  • Cell Line
  • Mice
  • Mutation
  • Neurofibromin 2
  • Phosphorylation
  • Plasmids
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases
  • Serine
  • Signal Transduction
  • Subcellular Fractions
  • Swine
  • Time Factors
  • Transfection
  • cdc42 GTP-Binding Protein
  • p21-Activated Kinases
  • Digital Object Identifier (doi)

    Pubmed Id

  • 11782491
  • Start Page

  • 10394
  • End Page

  • 10399
  • Volume

  • 277
  • Issue

  • 12