W. Vancriekinge et al., FUNCTIONAL-CHARACTERIZATION OF THE PRODOMAIN OF INTERLEUKIN-1-BETA-CONVERTING ENZYME, The Journal of biological chemistry, 271(44), 1996, pp. 27245-27248
Interleukin 1 beta-converting enzyme (ICE) has been identified as the
main protease responsible for maturation of the prodomain of interleuk
in-1 beta. Recently, it was shown to belong to a larger gene family, m
embers of which play an important role in programmed cell death. A com
mon feature of the ICE family proteases is the presence of a prodomain
that has been hypothesized to keep the enzyme in an inactive form. Ex
pression analysis in yeast revealed autocatalytic degradation of p45IC
E, but not of p30ICE lacking a prodomain. We further demonstrate that
p45ICE, in which the critical cysteine has been mutated, is still able
to dimerize in vivo, Dimerization requires the prodomain and occurs p
rior to autoprocessing. These results provide evidence for a regulator
y role of the prodomain of ICE.