The human mitotic kinesin KIF18A binds protein phosphatase 1 (PP1) through a highly conserved docking motif

Biochem Biophys Res Commun. 2014 Oct 24;453(3):432-7. doi: 10.1016/j.bbrc.2014.09.105. Epub 2014 Oct 1.

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.

Keywords: KIF18A; Kinesin; Klp5/6; Mitosis; Molecular evolution; Protein phosphatase 1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • HeLa Cells
  • Humans
  • Kinesins / metabolism*
  • Mitosis*
  • Phylogeny
  • Protein Phosphatase 1 / metabolism*

Substances

  • Protein Phosphatase 1
  • KIF18A protein, human
  • Kinesins