CK1 is required for a mitotic checkpoint that delays cytokinesis.

Johnson AE, Chen JS, Gould KL
Curr Biol. 2013 23 (19): 1920-6

PMID: 24055157 · PMCID: PMC4078987 · DOI:10.1016/j.cub.2013.07.077

Failure to accurately partition genetic material during cell division causes aneuploidy and drives tumorigenesis. Cell-cycle checkpoints safeguard cells from such catastrophes by impeding cell-cycle progression when mistakes arise. FHA-RING E3 ligases, including human RNF8 and CHFR and fission yeast Dma1, relay checkpoint signals by binding phosphorylated proteins via their FHA domains and promoting ubiquitination of downstream targets. Upon mitotic checkpoint activation, S. pombe Dma1 concentrates at spindle pole bodies (SPBs) in an FHA-dependent manner and ubiquitinates Sid4, a scaffold of Polo kinase, to suspend cytokinesis. However, the kinase or kinases that phosphoprime Sid4 for Dma1-mediated ubiquitination are unknown. Here, we report that the highly conserved protein kinase CK1 transmits the signal necessary to stall cytokinesis by phosphopriming Sid4 for Dma1-mediated ubiquitination. Like Dma1, CK1 accumulates at SPBs during a mitotic arrest and associates stably with SPB components, including Sid4. Our results establish CK1 as an integral component of a mitotic, ubiquitin-mediated checkpoint pathway.

Copyright © 2013 Elsevier Ltd. All rights reserved.

MeSH Terms (16)

Casein Kinase I Cell Cycle Proteins Cell Division Cytokinesis Green Fluorescent Proteins Microtubule-Associated Proteins M Phase Cell Cycle Checkpoints Nuclear Proteins Phosphorylation Protein-Serine-Threonine Kinases Protein Kinases Schizosaccharomyces Schizosaccharomyces pombe Proteins Signal Transduction Spindle Pole Bodies Ubiquitination

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