Regulation of procaspase-2 by glucocorticoid modulatory element-binding protein 1 through the interaction with caspase recruitment domain.
Caspases are the primary executioners of apoptosis. Although procaspases believe to exist as inactive forms in cells, the detailed regulatory system remains unclear. Here we show that glucocorticoid modulatory element-binding protein 1 (GMEB1) is capable of binding to the prodomain of caspase-2. We found that this molecule inhibits the autoproteolytic activation of procaspase-2 by oligomerization on a chemical compound-dependent system. These findings indicated that GMEB1 might be an endogenous inhibitory protein that selectively interacts with prodomain of caspase-2 to disrupt the autoactivation.
Tsuruma
Kazuhiro
K
Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Hokkaido University, N12W6, Sapporo 060-0812, Japan.
Nakagawa
Tadashi
T
Shirakura
Hiromi
H
Hayashi
Naoko
N
Uehara
Takashi
T
Nomura
Yasuyuki
Y
D017209:Apoptosis; D053143:Caspase 2; D020169:Caspases / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004789:Enzyme Activation; D005786:Gene Expression Regulation; D006367:HeLa Cells; D006801:Humans; D007668:Kidney / Q000378:metabolism*; D009703:Nucleoside-Phosphate Kinase / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*
D004268:DNA-Binding Proteins; D011994:Recombinant Proteins; D014157:Transcription Factors; C400298:p96 subunit, parvovirus initiation factor; D009703:Nucleoside-Phosphate Kinase; D053143:Caspase 2; D020169:Caspases