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KLF6 degradation after apoptotic DNA damage
Author(s) -
Banck Michaela S.,
Beaven Simon W.,
Narla Goutham,
Walsh Martin J.,
Friedman Scott L.,
Beutler Andreas S.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.077
Subject(s) - apoptosis , proteasome , cancer research , dna damage , mdm2 , programmed cell death , caspase , cisplatin , microbiology and biotechnology , ubiquitin , intrinsic apoptosis , chemistry , biology , gene , dna , genetics , biochemistry , chemotherapy
Krüppel‐like factor 6 (KLF6) is a cancer gene ( www.sanger.ac.uk/genetics/CGP/Census/ ). Here, we demonstrate that KLF6 protein is rapidly degraded when apoptosis is induced via the intrinsic pathway by cisplatin, adriamycin, or UVB irradiation in multiple cell lines (HCT116, SW40, HepG2, PC3‐M, Skov3, NIH‐3T3, 293T, GM09706, and MEF, IMR‐90). KLF6 degradation occurred in the presence or absence of p53, was associated with ubiquitination, mediated by the proteasome (half‐life 16 min, unstimulated), and independent of caspases and calpain. KLF6 was unchanged by apoptosis via the extrinsic/death‐receptor pathway. Deregulation of KLF6 stability may alter its tumor suppressor function and/or the response of tumors to chemotherapeutics.