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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.

Original publication

DOI

10.1038/nrm1621

Type

Journal article

Publication Date

04/2005

Volume

6

Pages

287 - 297

Keywords

Animals, Caspases, Humans, Inhibitor of Apoptosis Proteins, Protein Structure, Tertiary, Proteins, Tumor Necrosis Factor Receptor-Associated Peptides and Proteins, Ubiquitin, Ubiquitin-Protein Ligases