[HTML][HTML] Apoptosis promotes a caspase-induced amino-terminal truncation of IκBα that functions as a stable inhibitor of NF-κB
JY Reuther, AS Baldwin - Journal of Biological Chemistry, 1999 - ASBMB
Caspases are cell death cysteine proteases that are activated upon the induction of the
apoptotic program and cleave target proteins in a sequence-specific manner to promote cell
death. Recently, Barkett et al.(Barkett, M., Xue, D., Horvitz, HR, and Gilmore, TD (1997) J.
Biol. Chem. 272, 29419–29422) have shown that IκBα, the inhibitory subunit of the
transcription factor NF-κB, can be cleaved by caspase-3 in vitro at a site that potentially
produces a dominant inhibitory form of IκBα. The involvement of NF-κB in the inhibition of …
apoptotic program and cleave target proteins in a sequence-specific manner to promote cell
death. Recently, Barkett et al.(Barkett, M., Xue, D., Horvitz, HR, and Gilmore, TD (1997) J.
Biol. Chem. 272, 29419–29422) have shown that IκBα, the inhibitory subunit of the
transcription factor NF-κB, can be cleaved by caspase-3 in vitro at a site that potentially
produces a dominant inhibitory form of IκBα. The involvement of NF-κB in the inhibition of …