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Updated: Apr 23, 2026

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
Published on: September 28, 2018
The human mitotic kinesin KIF18A binds protein phosphatase 1 (PP1) through a highly conserved docking motif
Veerle De Wever1, Isha Nasa1, Delphine Chamousset2
1Department of Biological Sciences, University of Calgary, 2500 University Dr., Calgary, Alberta T2N 1N4, Canada.
Abstract:
Protein phosphatase 1 (PP1), a serine/threonine protein phosphatase, controls diverse key cellular events. PP1 catalytic subunits form complexes with a variety of interacting proteins that control its ability to dephosphorylate substrates. Here we show that the human mitotic kinesin-8, KIF18A, directly interacts with PP1γ through a conserved RVxF motif. Our phylogenetic analyses of the kinesins further uncovered the broad conservation of this interaction potential within the otherwise highly diverse motor-protein superfamily. This suggests an ancestral origin of PP1 recruitment to KIF18A and a strategic role in human mitotic cells.
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