Abstract
The inhibitors of apoptosis proteins (IAPs) are endogenous inhibitors for apoptosis. Apoptosis is carried out by caspases, which are the family of cystein proteases. IAPs regulate caspases through two conserved regions, the baculovirus IAP repeats (BIRs) and the really interesting new gene (RING) domains. Although the BIRs are responsible for binding to caspases, the RING domain can act as a ubiquitin-E3 ligase, leading to ubiquitylation of IAPs themselves and their pro-apoptotic IAP counterparts such as caspases. Recently, it is reported that another ubiquitin-like protein, neuronal precursor cell-expressed developmentally downregulated protein 8 (NEDD8), is also involved in the regulation of apoptosis through neddylation of caspases mediated by IAPs. On the contrary, the results against the function of IAPs as a NEDD8-E3 ligase are also suggested. This review presents the summary of IAPs, caspases, and the ubiquitin-proteasome system and how their interactions influence the regulation of apoptosis.
About the author
Shinji Kamada received a PhD in Medical Science from Osaka University, Japan. He had worked as a postdoctoral fellow and an assistant professor at Osaka University, as a research fellow at The Salk Institute, and as a COE senior research fellow at Kobe University. Since 2007, Dr. Kamada has been an associate professor at Biosignal Research Center, Kobe University, Japan. His work has been focused on the molecular mechanisms of apoptosis.
©2013 by Walter de Gruyter Berlin Boston
