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KMID : 0613820070170081063
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Journal of Life Science
2007 Volume.17 No. 8 p.1063 ~ p.1067
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Mcl-1 is a Binding Partner of hNoxa
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Park Sun-Young
Kim Tae-Hyoung
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Abstract
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The Bcl-2 family proteins play critical roles in regulation of apoptosis, and the balanced interaction of pro- and anti-death members is a key factor in determining the cell fate. Noxa, a BH3-only Bcl-2-family member, has been originally identified as a target gene of p53. To understand the mechanism by which human Noxa (hNoxa) regulates the cell death, we screened the hNoxa binding partner using the yeast two hybrid screening and found that anti-death protein Mcl-1 binds to hNoxa. The binding of hNoxa to Mcl-1 was confirmed by immunoprecipitation in human colon cancer cell line HCT 116 cells. Mcl-1 significantly inhibited the hNoxa-induced cell death in HCT 116 cells. During the cell death induced by hNoxa, Mcl-1 protein was degraded. Its degradation was inhibited by z-VAD-fmk, a pan-caspase inhibitor, suggesting caspase is responsible for Mcl-1 degradation in response to hNoxa. Together, the results indicate that hNoxa binds to Mcl-1 that is degraded by caspases during hNoxa-induced cell death.
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KEYWORD
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hNoxa, Mcl-1, Bcl-2 family, p53, apoptosis
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