You are currently viewing the editor's summary.
View Full TextLog in to view the full text
AAAS login provides access to Science for AAAS members, and access to other journals in the Science family to users who have purchased individual subscriptions.
More options
Download and print this article for your personal scholarly, research, and educational use.
Buy a single issue of Science for just $15 USD.
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.
This is an article distributed under the terms of the Science Journals Default License.
