Novel Insights into Chk1 Regulation by Phosphorylation

DOI Web Site PubMed 6 Citations 84 References Open Access
  • Goto Hidemasa
    Division of Biochemistry, Aichi Cancer Center Research Institute Department of Cellular Oncology, Nagoya University Graduate School of Medicine
  • Kasahara Kousuke
    Division of Biochemistry, Aichi Cancer Center Research Institute Department of Oncology, Graduate School of Pharmaceutical Sciences, Nagoya City University
  • Inagaki Masaki
    Division of Biochemistry, Aichi Cancer Center Research Institute Department of Cellular Oncology, Nagoya University Graduate School of Medicine

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Abstract

Checkpoint kinase 1 (Chk1) is a conserved protein kinase central to the cell-cycle checkpoint during DNA damage response (DDR). Until recently, ATR, a protein kinase activated in response to DNA damage or stalled replication, has been considered as the sole regulator of Chk1. Recent progress, however, has led to the identification of additional protein kinases involved in Chk1 phosphorylation, affecting the subcellular localization and binding partners of Chk1. In fact, spatio-temporal regulation of Chk1 is of critical importance not only in the DDR but also in normal cell-cycle progression. In due course, many potent inhibitors targeted to Chk1 have been developed as anticancer agents and some of these inhibitors are currently in clinical trials. In this review, we summarize the current knowledge of Chk1 regulation by phosphorylation.

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