Palladin is a novel binding partner of ILKAP in eukaryotic cells

Biochem Biophys Res Commun. 2011 Aug 12;411(4):768-73. doi: 10.1016/j.bbrc.2011.07.022. Epub 2011 Jul 18.

Abstract

Palladin was a novel binding partner of ILKAP in eukaryotic cells. Palladin's C-terminal fragment including only its last three Ig domains (residues 710-1106) and the PP2C domain of ILKAP (residues 108-392) were necessary and sufficient for their interaction. The biological significance of the interaction between palladin and ILKAP was that palladin recruited the cytoplasmic ILKAP to initiate ILKAP-induced apoptosis. Our results suggested that palladin played a specific role in modulating the subcellular localization of the cytoplasmic ILKAP and promoting the ILKAP-induced apoptosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis*
  • COS Cells
  • Chlorocebus aethiops
  • Cytoplasm / enzymology
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • Eukaryotic Cells / metabolism
  • Gene Knockdown Techniques
  • HEK293 Cells
  • Humans
  • Phosphoprotein Phosphatases / genetics
  • Phosphoprotein Phosphatases / metabolism*
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Two-Hybrid System Techniques

Substances

  • Cytoskeletal Proteins
  • PALLD protein, human
  • Phosphoproteins
  • ILKAP protein, human
  • Phosphoprotein Phosphatases