Novel Insights into Chk1 Regulation by Phosphorylation

DOI Web Site PubMed 被引用文献6件 参考文献84件 オープンアクセス
  • 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

この論文をさがす

抄録

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.

収録刊行物

被引用文献 (6)*注記

もっと見る

参考文献 (84)*注記

もっと見る

関連プロジェクト

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ