Research ArticleMitosis

Aurora B opposes PP1 function in mitosis by phosphorylating the conserved PP1-binding RVxF motif in PP1 regulatory proteins

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Science Signaling  15 May 2018:
Vol. 11, Issue 530, eaai8669
DOI: 10.1126/scisignal.aai8669

Yin and yang of mitotic phosphorylation

Mitotic kinases promote cell cycle progression by targeting a large set of proteins that collectively drive mitosis. Phosphatases, such as protein phosphatase 1 (PP1), reverse these phosphorylation events to enable cells to exit mitosis. The subcellular localization and activity of PP1 are controlled by regulatory proteins that bind to PP1 through conserved RVxF motifs. Nasa et al. found that RVxF motifs in a subset of PP1 regulatory proteins in which the “x” residue is a serine or threonine (RV[S/T]F) were phosphorylated during mitosis. Phosphorylation of these motifs, which was mediated primarily by the mitotic kinase Aurora B, prevented proteins that harbored these motifs from interacting with PP1 and was required for maintaining the high amount of overall protein phosphorylation in mitotic cells. These findings identify a mechanism that coordinates the activities of Aurora B and PP1 to control cell cycle progression.

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