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- Title
X-linked inhibitor of apoptosis protein mediates neddylation by itself but does not function as a NEDD8–E3 ligase for caspase-7
- Authors
Nagano, Taiki; Hashimoto, Toshiaki; Nakashima, Akio; Kikkawa, Ushio; Kamada, Shinji
- Abstract
Abstract: X-linked inhibitor of apoptosis protein (XIAP) is a potent antagonist of caspases, and functions as a ubiquitin–E3 ligase by itself and for caspases. Recently, NEDD8, a ubiquitin-like modifier, has been suggested to be used for modification of caspase-7 mediated by XIAP. However, it is not clear whether caspase-7 is a bona fide target for NEDD8. Here we showed that no neddylation of caspase-7 but that of XIAP itself was observed under the conditions in which caspase-7 was modified with ubiquitin. These results reveal that XIAP does not function as a NEDD8–E3 ligase for caspase-7 in vivo. Structured summary of protein interactions: NEDD8 physically interacts with Caspase-7 by pull down ( View interaction ) XIAP physically interacts with NEDD8 by anti-bait coimmunoprecipitation ( View interaction )
- Subjects
UBIQUITIN; CASPASES; X-linked inhibitor of apoptosis protein; PROTEIN-protein interactions; CELL physiology; CELLULAR control mechanisms; HEMAGGLUTININ
- Publication
FEBS Letters, 2012, Vol 586, Issue 11, p1612
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2012.04.056