IAPs, RINGs and ubiquitylation.
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.
Vaux
David L
DL
The Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Victoria 3050, Australia. vaux@wehi.edu.au
Silke
John
J
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
D051034:Inhibitor of Apoptosis Proteins; D011506:Proteins; D047988:Tumor Necrosis Factor Receptor-Associated Peptides and Proteins; D025801:Ubiquitin; D044767:Ubiquitin-Protein Ligases; D020169:Caspases