title: IAPs, RINGs and ubiquitylation.
abstract: The inhibitor of apoptosis (IAP) proteins all contain one or more baculoviral IAP repeat motifs, through which they interact with various other proteins. Many IAPs also have another zinc-binding motif, the RING domain, which can recruit E2 ubiquitin-conjugating enzymes and catalyse the transfer of ubiquitin onto target proteins. The number of targets of IAP-mediated ubiquitylation is increasing and recent results indicate that outcomes following ubiquitylation are tantalizingly complex. As well as regulating other proteins, the IAPs themselves are controlled by ubiquitin-mediated degradation.
authors.affiliation: The Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Victoria 3050, Australia. vaux@wehi.edu.au
authors.forename: David L
authors.initials: DL
authors.lastname: Vaux
authors.forename: John
authors.initials: J
authors.lastname: Silke
mesh_terms: D000818:Animals; D020169:Caspases / Q000378:metabolism; D006801:Humans; D051034:Inhibitor of Apoptosis Proteins; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D047988:Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / Q000378:metabolism; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism
chemical_list: D051034:Inhibitor of Apoptosis Proteins; D011506:Proteins; D047988:Tumor Necrosis Factor Receptor-Associated Peptides and Proteins; D025801:Ubiquitin; D044767:Ubiquitin-Protein Ligases; D020169:Caspases