title: Caspase-9 swings both ways in the apoptosome.
abstract: For nearly 2 decades, investigators have debated whether cysteinyl-aspartate-specific protease 9 (caspase-9) is activated within the apoptotic protease-activating factor 1 (Apaf-1) apoptosome through proximity-induced homodimerization or through formation of a holoenzyme. Recently, we have demonstrated that caspase-9 forms (and likely transitions between) both caspase-9 homo- and Apaf-1:caspase-9 heterodimers, each of which plays unique roles in the recruitment and activation of caspase-9.
authors.affiliation: Department of Epigenetics and Molecular Carcinogenesis, The University of Texas MD Anderson Cancer Center , Smithville, TX, USA.
authors.forename: Chu-Chiao
authors.initials: CC
authors.lastname: Wu
authors.affiliation: Department of Epigenetics and Molecular Carcinogenesis, The University of Texas MD Anderson Cancer Center , Smithville, TX, USA.
authors.forename: Shawn B
authors.initials: SB
authors.lastname: Bratton
keywords: Apaf-1; apoptosome; caspase-3; caspase-9; molecular timer