IAPs, RINGs and ubiquitylation

Author(s): Vaux, DL; Silke, J;
Details: Publication Year 2005-04,Volume 6,Issue #4,Page 287-297
Journal Title: NATURE REVIEWS MOLECULAR CELL BIOLOGY
Publication Type: Journal Article
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.
Publisher: NATURE PUBLISHING GROUP
Keywords: UBIQUITIN-PROTEIN LIGASE; KAPPA-B ACTIVATION; ANTI-APOPTOTIC ACTIVITY; PROGRAMMED CELL-DEATH; X-LINKED INHIBITOR; SERINE-PROTEASE; IN-VITRO; U-BOX; BACULOVIRAL-INHIBITOR; CONJUGATING ENZYMES
Publisher's Version: https://doi.org/10.1038/nrm1621
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2005-04-01 12:00:00