HSP70 colocalizes with PLK1 at the centrosome and disturbs spindle dynamics in cells arrested in mitosis by arsenic trioxide

Abstract

Heat shock protein 70 (HSP70) has been shown to be a substrate of Polo-like kinase 1 (PLK1), and it prevents cells arrested in mitosis by arsenic trioxide (ATO) from dying. Here, we report that HSP70 participates in ATO-induced spindle elongation, which interferes with mitosis progression. Our results demonstrate that HSP70 and PLK1 colocalize at the… (More)
DOI: 10.1007/s00204-014-1222-x

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@article{Chen2014HSP70CW, title={HSP70 colocalizes with PLK1 at the centrosome and disturbs spindle dynamics in cells arrested in mitosis by arsenic trioxide}, author={Yi-Ju Chen and Kuo-Chu Lai and H. -C. Kuo and Lu-Ping Chow and L H Yih and Te-Chang Lee}, journal={Archives of Toxicology}, year={2014}, volume={88}, pages={1711-1723} }