Caspase activation, inhibition, and reactivation: a mechanistic view.
Caspases, a unique family of cysteine proteases, execute programmed cell death (apoptosis). Caspases exist as inactive zymogens in cells and undergo a cascade of catalytic activation at the onset of apoptosis. The activated caspases are subject to inhibition by the inhibitor-of-apoptosis (IAP) family of proteins. This inhibition can be effectively removed by diverse proteins that share an IAP-binding tetrapeptide motif. Recent structural and biochemical studies have revealed the underlying molecular mechanisms for these processes in mammals and in Drosophila. This paper reviews these latest advances.
Shi
Yigong
Y
Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, Princeton, New Jersey 08544, USA. yshi@molbio.princeton.edu
D020816:Amino Acid Motifs; D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D020169:Caspases / Q000737:chemistry* / Q000378:metabolism*; D004330:Drosophila / Q000378:metabolism; D004789:Enzyme Activation / Q000502:physiology; D004793:Enzyme Reactivators / Q000378:metabolism; D006801:Humans; D051034:Inhibitor of Apoptosis Proteins; D008322:Mammals / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
D004793:Enzyme Reactivators; D051034:Inhibitor of Apoptosis Proteins; D011506:Proteins; D020169:Caspases