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• W25687112 abstract "Research Article1 July 1996free access DNA-dependent protein kinase catalytic subunit: a target for an ICE-like protease in apoptosis. Q. Song Q. Song Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author S. P. Lees-Miller S. P. Lees-Miller Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author S. Kumar S. Kumar Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author Z. Zhang Z. Zhang Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author D. W. Chan D. W. Chan Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author G. C. Smith G. C. Smith Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author S. P. Jackson S. P. Jackson Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author E. S. Alnemri E. S. Alnemri Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author G. Litwack G. Litwack Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author K. K. Khanna K. K. Khanna Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author M. F. Lavin M. F. Lavin Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author Q. Song Q. Song Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author S. P. Lees-Miller S. P. Lees-Miller Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author S. Kumar S. Kumar Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author Z. Zhang Z. Zhang Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author D. W. Chan D. W. Chan Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author G. C. Smith G. C. Smith Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author S. P. Jackson S. P. Jackson Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author E. S. Alnemri E. S. Alnemri Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author G. Litwack G. Litwack Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author K. K. Khanna K. K. Khanna Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author M. F. Lavin M. F. Lavin Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. Search for more papers by this author Author Information Q. Song1, S. P. Lees-Miller1, S. Kumar1, Z. Zhang1, D. W. Chan1, G. C. Smith1, S. P. Jackson1, E. S. Alnemri1, G. Litwack1, K. K. Khanna1 and M. F. Lavin1 1Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia. The EMBO Journal (1996)15:3238-3246https://doi.org/10.1002/j.1460-2075.1996.tb00688.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Radiosensitive cell lines derived from X-ray cross complementing group 5 (XRCC5), SCID mice and a human glioma cell line lack components of the DNA-dependent protein kinase, DNA-PK, suggesting that DNA-PK plays an important role in DNA double-strand break repair. Another enzyme implicated in DNA repair, poly(ADP-ribose) polymerase, is cleaved and inactivated during apoptosis, suggesting that some DNA repair proteins may be selectively targeted for destruction during apoptosis. Here we demonstrate that DNA-PKcs, the catalytic subunit of DNA-PK, is preferentially degraded after the exposure of different cell types to a variety of agents known to cause apoptosis. However, Ku, the DNA-binding component of the enzyme, remains intact. Degradation of DNA-PKcs was accompanied by loss of DNA-PK activity. One cell line resistant to etoposide-induced apoptosis failed to show degradation of DNA-PKcs. Protease inhibitor data implicated an ICE-like protease in the cleavage of DNA-PKcs, and it was subsequently shown that the cysteine protease CPP32, but not Mch2alpha, ICE or TX, cleaved purified DNA-PKcs into three fragments of comparable size with those observed in cells undergoing apoptosis. Cleavage sites in DNA-PKcs, determined by antibody mapping and microsequencing, were shown to be the same for CPP32 cleavage and for cleavage catalyzed by extracts from cells undergoing apoptosis. These observations suggest that DNA-PKcs is a critical target for proteolysis by an ICE-like protease during apoptosis. Previous ArticleNext Article Volume 15Issue 131 July 1996In this issue RelatedDetailsLoading ..." @default.
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• W25687112 title "DNA-dependent protein kinase catalytic subunit: a target for an ICE-like protease in apoptosis." @default.
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• W25687112 doi "https://doi.org/10.1002/j.1460-2075.1996.tb00688.x" @default.
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