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https://hdl.handle.net/2440/8786
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dc.contributor.author | Song, Q. | - |
dc.contributor.author | Lees-Miller, S. | - |
dc.contributor.author | Kumar, S. | - |
dc.contributor.author | Zhang, N. | - |
dc.contributor.author | Chan, D. | - |
dc.contributor.author | Smith, G. | - |
dc.contributor.author | Jackson, S. | - |
dc.contributor.author | Alnemri, E. | - |
dc.contributor.author | Litwack, G. | - |
dc.contributor.author | Khanna, K. | - |
dc.contributor.author | Lavin, M. | - |
dc.date.issued | 1996 | - |
dc.identifier.citation | The EMBO Journal, 1996; 15(13):3238-3246 | - |
dc.identifier.issn | 0261-4189 | - |
dc.identifier.issn | 1460-2075 | - |
dc.identifier.uri | http://hdl.handle.net/2440/8786 | - |
dc.description.abstract | 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. | - |
dc.description.statementofresponsibility | Song, Q ; Lees-miller, S P ; Kumar, S ; Zhang, Z ; Chan, D W ; Smith, G C ; Jackson, S P ; Alnemri, E S ; Litwack, G ; Khanna, K K ; Lavin, M F | - |
dc.language.iso | en | - |
dc.publisher | OXFORD UNIV PRESS UNITED KINGDOM | - |
dc.source.uri | http://dx.doi.org/10.1002/j.1460-2075.1996.tb00688.x | - |
dc.subject | Cell Line | - |
dc.subject | Hela Cells | - |
dc.subject | Tumor Cells, Cultured | - |
dc.subject | Animals | - |
dc.subject | Humans | - |
dc.subject | Mice | - |
dc.subject | Mice, SCID | - |
dc.subject | Etoposide | - |
dc.subject | Cysteine Endopeptidases | - |
dc.subject | Caspase 1 | - |
dc.subject | DNA-Binding Proteins | - |
dc.subject | Nuclear Proteins | - |
dc.subject | DNA Primers | - |
dc.subject | Antibodies | - |
dc.subject | Apoptosis | - |
dc.subject | Base Sequence | - |
dc.subject | Substrate Specificity | - |
dc.subject | Hydrolysis | - |
dc.subject | Catalysis | - |
dc.subject | Molecular Sequence Data | - |
dc.subject | DNA-Activated Protein Kinase | - |
dc.subject | Protein Serine-Threonine Kinases | - |
dc.title | DNA-dependent protein kinase catalytic subunit: a target for an ICE-like protease in apoptosis | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1002/j.1460-2075.1996.tb00688.x | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Kumar, S. [0000-0001-7126-9814] | - |
Appears in Collections: | Aurora harvest 4 Medicine publications |
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