The ubiquitin ligase ability of IAPs regulates apoptosis.
Accumulating evidence indicates that there is a critical role of the ubiquitin/proteasome pathway in the regulation of apoptosis. Among the important molecules that couple these two fundamental cellular activities are members of the inhibitor of apoptosis (IAP) protein family. In addition to their well-studied ability to directly bind and inhibit caspases, many IAPs contain RING domains that are necessary and sufficient to cause ubiquitylation and subsequent proteasome-mediated proteolysis. This review summarizes recent findings about the ubiquitin protein ligase activity of IAPs, and considers possible mechanisms for substrate selectivity.
Ni
Ting
T
College of Life Science, Sichuan University, Sichuan Province, P. R. China.
Li
Wenjing
W
Zou
Fangdong
F
D017209:Apoptosis / Q000235:genetics*; D051017:Apoptosis Regulatory Proteins; D020169:Caspases / Q000378:metabolism*; D040461:Gene Components; D051034:Inhibitor of Apoptosis Proteins / Q000235:genetics / Q000378:metabolism*; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism; D024101:Mitochondrial Proteins / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics*; D015398:Signal Transduction / Q000235:genetics*; D013379:Substrate Specificity; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*
D051017:Apoptosis Regulatory Proteins; C412403:DIABLO protein, human; D051034:Inhibitor of Apoptosis Proteins; D047908:Intracellular Signaling Peptides and Proteins; D024101:Mitochondrial Proteins; D044767:Ubiquitin-Protein Ligases; D020169:Caspases