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Binding of Kif23-iso1/CHO1 to 14-3-3 is regulated by sequential phosphorylations at two LATS kinase consensus sites. | LitMetric

AI Article Synopsis

  • * The study reveals that for proper phosphorylation at one site (S814), a preceding phosphorylation at S716 (only in CHO1) is necessary, indicating a specific order of phosphorylation for Kif23's function.
  • * Furthermore, Kif23 shows little phosphorylation at S814 in the midbodies after cell division, suggesting this modification could be used to identify these structures in further research.

Article Abstract

Kif23 kinesin is an essential actor of cytokinesis in animals. It exists as two major isoforms, known as MKLP1 and CHO1, the longest of which, CHO1, contains two HXRXXS/T NDR/LATS kinase consensus sites. We demonstrate that these two sites are readily phosphorylated by NDR and LATS kinases in vitro, and this requires the presence of an upstream -5 histidine residue. We further show that these sites are phosphorylated in vivo and provide evidence revealing that LATS1,2 participate in the phosphorylation of the most C-terminal S814 site, present on both isoforms. This S814 phosphosite was previously reported to constitute a 14-3-3 binding site, which plays a role in Kif23 clustering during cytokinesis. Surprisingly, we found that phosphorylation of the upstream S716 NDR/LATS consensus site, present only in the longest Kif23 isoform, is required for efficient phosphorylation at S814, thus revealing sequential phosphorylation at these two sites, and differential regulation of Kif23-14-3-3 interaction for the two Kif23 isoforms. Finally, we provide evidence that Kif23 is largely unphosphorylated on S814 in post-abscission midbodies, making this Kif23 post-translational modification a potential marker to probe these structures.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4320110PMC
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0117857PLOS

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