Author: Jeon, Young Joo; Park, Jong Ho; Chung, Chin Ha
Title: Interferon-Stimulated Gene 15 in the Control of Cellular Responses to Genotoxic Stress Document date: 2017_2_28
ID: w731ehtz_20
Snippet: DNA-damaging agents, such as camptothecin and doxorubicin, induce ISGylation of ï„Np63ï¡ in MCF10A and various epithelial cancer cell lines, including HNSCC013, HCC1937, and FaDu (Jeon et al., 2012) . Lys139 and Lys324 serve as the ISGylation sites in ï„Np63ï¡. Upon exposure to the DNA-damaging agents, caspase-2 is activated, although with an unknown mechanism(s), and cleaves off the TI domain from ISGylated ï„Np63ï¡, but not from its unmod.....
Document: DNA-damaging agents, such as camptothecin and doxorubicin, induce ISGylation of ï„Np63ï¡ in MCF10A and various epithelial cancer cell lines, including HNSCC013, HCC1937, and FaDu (Jeon et al., 2012) . Lys139 and Lys324 serve as the ISGylation sites in ï„Np63ï¡. Upon exposure to the DNA-damaging agents, caspase-2 is activated, although with an unknown mechanism(s), and cleaves off the TI domain from ISGylated ï„Np63ï¡, but not from its unmodified form, suggesting that ISG15 molecules conjugated to ï„Np63ï¡ act as molecular scaffolds for recruiting activated caspase-2. Asp452, Asp469, and Asp489 are the cleavage sites in ï„Np63ï¡. The cleaved TI domain is exported to the cytoplasm from the nucleus, thus losing its ability to bind the TA domain and inhibit the transcriptional activity of TA domain-containing p53 family members in the nucleus. Under the same stress conditions, TAp63ï¡, is also ISGylated and cleaved by caspase-2 and its TI domain is released to the cytoplasm, thus yielding a transcriptionally active form of TAp63ï¡.
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