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KMID : 0624620110440050352
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BMB Reports
2011 Volume.44 No. 5 p.352 ~ p.357
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Knock-down of human MutY homolog (hMYH) decreases phosphorylation of checkpoint kinase 1 (Chk1) induced by hydroxyurea and UV treatment
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Hahm Soo-Hyun
Park Jong-Hwa
Ko Sung-Il
Lee You-Ri
Chung In-Sik
Chung Ji-Hyung
Kang Lin-Woo
Han Ye-Sun
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Abstract
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The effect of human MutY homolog (hMYH) on the activation of checkpoint proteins in response to hydroxyurea (HU) and ultraviolet (UV) treatment was investigated in hMYH-disrupted HEK293 cells. hMYH-disrupted cells decreased the phosphorylation of Chk1 upon HU or UV treatment and increased the phosphorylation of Cdk2 and the amount of Cdc25A, but not Cdc25C. In siMYH-transfected cells, the increased rate of phosphorylated Chk1 upon HU or UV treatment was lower than that in siGFP-transfected cells, meaning that hMYH was involved in the activation mechanism of Chk1 upon DNA damage. The phosphorylation of ataxia telangiectasia and Rad3- related protein (ATR) upon HU or UV treatment was decreased in hMYH-disrupted HEK293 and HaCaT cells. Co-immunoprecipitation experiments showed that hMYH was immunoprecipitated by anti-ATR. These results suggest that hMYH may interact with ATR and function as a mediator of Chk1 phosphorylation in response to DNA damage.
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KEYWORD
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Ataxia telangiectasia and Rad3-related protein (ATR), Checkpoint kinase 1 (Chk1), Human MutY homolog (hMYH), Hydroxyurea
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