RRC ID 45864
著者 Tavernier N, Noatynska A, Panbianco C, Martino L, Van Hove L, Schwager F, Léger T, Gotta M, Pintard L.
タイトル Cdk1 phosphorylates SPAT-1/Bora to trigger PLK-1 activation and drive mitotic entry in C. elegans embryos.
ジャーナル J Cell Biol
Abstract The molecular mechanisms governing mitotic entry during animal development are incompletely understood. Here, we show that the mitotic kinase CDK-1 phosphorylates Suppressor of Par-Two 1 (SPAT-1)/Bora to regulate its interaction with PLK-1 and to trigger mitotic entry in early Caenorhabditis elegans embryos. Embryos expressing a SPAT-1 version that is nonphosphorylatable by CDK-1 and that is defective in PLK-1 binding in vitro present delays in mitotic entry, mimicking embryos lacking SPAT-1 or PLK-1 functions. We further show that phospho-SPAT-1 activates PLK-1 by triggering phosphorylation on its activator T loop in vitro by Aurora A. Likewise, we show that phosphorylation of human Bora by Cdk1 promotes phosphorylation of human Plk1 by Aurora A, suggesting that this mechanism is conserved in humans. Our results suggest that CDK-1 activates PLK-1 via SPAT-1 phosphorylation to promote entry into mitosis. We propose the existence of a positive feedback loop that connects Cdk1 and Plk1 activation to ensure a robust control of mitotic entry and cell division timing.
巻・号 208(6)
ページ 661-9
公開日 2015-3-16
DOI 10.1083/jcb.201408064
PII jcb.201408064
PMID 25753036
PMC PMC4362466
MeSH Amino Acid Sequence Animals Aurora Kinase A / metabolism CDC2 Protein Kinase / physiology* Caenorhabditis elegans / cytology* Caenorhabditis elegans / enzymology Caenorhabditis elegans Proteins / metabolism* Cell Cycle Proteins / metabolism* Embryo, Nonmammalian / cytology Embryo, Nonmammalian / metabolism Enzyme Activation Humans Larva / cytology Larva / enzymology Mitosis Molecular Sequence Data Phosphorylation Protein Processing, Post-Translational Protein Serine-Threonine Kinases / metabolism* Sf9 Cells Spodoptera
IF 8.811
引用数 23
WOS 分野 CELL BIOLOGY
リソース情報
線虫 tm3061 tm3060