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Cdc7 kinase stimulates Aurora B kinase in M-phase

S. Ito, H. Goto, K. Kuniyasu, M. Shindo, M. Yamada, K. Tanaka, GT. Toh, M. Sawa, M. Inagaki, J. Bartek, H. Masai,

. 2019 ; 9 (1) : 18622. [pub] 20191209

Jazyk angličtina Země Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc20028718

The conserved serine-threonine kinase, Cdc7, plays a crucial role in initiation of DNA replication by facilitating the assembly of an initiation complex. Cdc7 is expressed at a high level and exhibits significant kinase activity not only during S-phase but also during G2/M-phases. A conserved mitotic kinase, Aurora B, is activated during M-phase by association with INCENP, forming the chromosome passenger complex with Borealin and Survivin. We show that Cdc7 phosphorylates and stimulates Aurora B kinase activity in vitro. We identified threonine-236 as a critical phosphorylation site on Aurora B that could be a target of Cdc7 or could be an autophosphorylation site stimulated by Cdc7-mediated phosphorylation elsewhere. We found that threonines at both 232 (that has been identified as an autophosphorylation site) and 236 are essential for the kinase activity of Aurora B. Cdc7 down regulation or inhibition reduced Aurora B activity in vivo and led to retarded M-phase progression. SAC imposed by paclitaxel was dramatically reversed by Cdc7 inhibition, similar to the effect of Aurora B inhibition under the similar situation. Our data show that Cdc7 contributes to M-phase progression and to spindle assembly checkpoint most likely through Aurora B activation.

Citace poskytuje Crossref.org

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$a The conserved serine-threonine kinase, Cdc7, plays a crucial role in initiation of DNA replication by facilitating the assembly of an initiation complex. Cdc7 is expressed at a high level and exhibits significant kinase activity not only during S-phase but also during G2/M-phases. A conserved mitotic kinase, Aurora B, is activated during M-phase by association with INCENP, forming the chromosome passenger complex with Borealin and Survivin. We show that Cdc7 phosphorylates and stimulates Aurora B kinase activity in vitro. We identified threonine-236 as a critical phosphorylation site on Aurora B that could be a target of Cdc7 or could be an autophosphorylation site stimulated by Cdc7-mediated phosphorylation elsewhere. We found that threonines at both 232 (that has been identified as an autophosphorylation site) and 236 are essential for the kinase activity of Aurora B. Cdc7 down regulation or inhibition reduced Aurora B activity in vivo and led to retarded M-phase progression. SAC imposed by paclitaxel was dramatically reversed by Cdc7 inhibition, similar to the effect of Aurora B inhibition under the similar situation. Our data show that Cdc7 contributes to M-phase progression and to spindle assembly checkpoint most likely through Aurora B activation.
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$a Goto, Hidemasa $u Department of Neural Regeneration and Cell Communication, Mie University Graduate School of Medicine, Tsu, Mie, 514-8507, Japan.
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$a Kuniyasu, Kinue $u Department of Molecular Oncology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, 980-8575, Japan.
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$a Shindo, Mayumi $u Laboratory of Protein Analyses, Tokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan.
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$a Yamada, Masayuki $u Medical Education Center, Graduate School of Medicine, Kyoto University, Kyoto, Japan. Institute of Molecular and Translational Medicine, Faculty of Medicine and Dentistry, Palacky University, 77900, Olomouc, Czech Republic.
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$a Tanaka, Kozo $u Department of Molecular Oncology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, 980-8575, Japan.
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$a Toh, Gaik-Theng $u Department of Genome Medicine, Tokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan.
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$a Bartek, Jiri $u Institute of Molecular and Translational Medicine, Faculty of Medicine and Dentistry, Palacky University, 77900, Olomouc, Czech Republic. Danish Cancer Society Research Center, Copenhagen, Denmark. Division of Genome Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.
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$a Masai, Hisao $u Department of Genome Medicine, Tokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan. masai-hs@igakuken.or.jp.
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