The p35 relative, p49, inhibits mammalian and Drosophila caspases including DRONC and protects against apoptosis

Author(s): Jabbour, AM; Ekert, PG; Coulson, EJ; Knight, MJ; Ashley, DM; Hawkins, CJ;
Details: Publication Year 2002-12,Volume 9,Issue #12,Page 1311-1320
Journal Title: CELL DEATH AND DIFFERENTIATION
Publication Type: Journal Article
Abstract: This study characterized the ability of a new member of the p35 family, p49, to inhibit a number of mammalian and insect caspases. p49 blocked apoptosis triggered by treatment with Fas ligand (FasL), Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) or ultraviolet (UV) radiation but provided negligible protection against apoptosis induced by the chemotherapeutic drug cisplatin. The caspase cleavage site in p49 was determined, and mutation of the 131 residue of this site abolished the ability of p49 to inhibit caspases, implying that p49 inhibits caspases through an analogous suicide-substrate mechanism to p35. Unlike p35, p49 inhibited the upstream insect caspase DRONC.
Publisher: NATURE PUBLISHING GROUP
Keywords: REACTIVE-SITE LOOP; BACULOVIRUS P35; CELL-DEATH; CRYSTAL-STRUCTURE; INSECT CELLS; IAP; EXPRESSION; MICE; GENE; CLEAVAGE
Publisher's Version: https://doi.org/10.1038/sj.cdd.4401135
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2002-12-01 12:00:00