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The mitotic kinase Aurora B is concentrated at the anaphase central spindle by the kinesin MKlp2 during mitotic exit and cytokinesis. This pool of Aurora B phosphorylates substrates including the kinesin KIF4A to regulate central spindle length. In this paper, we identify a counteracting system in which PP2A-B56γ and -ε, but not PP2A-B56α, -β, and -δ, are maintained at the central spindle by KIF4A. Biochemical assays show that PP2A-B56γ can dephosphorylate the T799 Aurora B site on KIF4A and thereby counteract the Aurora B- and microtubule-stimulated ATPase activity of KIF4A. In agreement with these observations, combined silencing of PP2A-B56γ and -ε resulted in increased phosphorylation of KIF4A T799 and decreased central spindle growth in anaphase B. Furthermore, reduced turnover of regulatory phosphorylation on another Aurora B substrate MKlp1 was observed, suggesting that PP2A-B56γ and -ε play a general role opposing Aurora B at the central spindle. KIF4A and PP2A-B56γ and -ε therefore create a spatially restricted negative feedback loop counteracting Aurora B in anaphase.

Original publication

DOI

10.1083/jcb.201409129

Type

Journal article

Journal

J Cell Biol

Publication Date

22/12/2014

Volume

207

Pages

683 - 693

Keywords

Anaphase, Animals, Aurora Kinase B, Feedback, Physiological, HeLa Cells, Humans, Kinesin, Protein Phosphatase 2, Protein Processing, Post-Translational, Protein Transport, Sf9 Cells, Spindle Apparatus, Spodoptera, Time-Lapse Imaging