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Updated: May 30, 2026

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics
Published on: July 6, 2014
Palladin is a novel binding partner of ILKAP in eukaryotic cells
Wang Zhou1, Shusen Cui, Shuhai Han
1Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun, PR China.
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.
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