Regulation of IAP-mediated apoptosis by the ubiquitin-proteasome pathway
Wei Li
Abstract:
Ubiquitin is a ubiquitously expressed 76 amino acid that can be covalently modify target proteins, leading to their ubiquitination. Many ubiquitination proteins are degraded by the 26S proteasome. Tightly and specifically regulated ubiquitin-proteasome pathway is essential for all organisms controlling cell cycle progression, signal transduction and cell survival. The apoptotic regulation via Ubiquitin system has been well established in animals. RING domain-containing members of IAP (inhibitor of apoptosis protein) family proteins can function as ubiquitin protein ligases to ubiquitinate their target proteins or promote autoubiqutination in animal apoptosis. Although cell death process between plants and animals is conserved, key regulators in animals have no homology in plants. However, conserved function of Sf-IAP from Spodoptera frugiperda (fall armyworm) was shown to inhibit cell death induced by several abiotic stresses and necrotrophic pathogen in my previous work. RING domain of IAPs as ubiquitin protein ligase is highly conserved in plants. The potential of Sf-IAP regulate cell death and development in plants by ubiquitin-proteasome pathway was discussed.