IAPs, RINGs and ubiquitylation

DL Vaux, J Silke - Nature reviews Molecular cell biology, 2005 - nature.com
Nature reviews Molecular cell biology, 2005nature.com
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 …
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.
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