X-linked inhibitor of apoptosis protein mediates neddylation by itself but does not function as a NEDD8-E3 ligase for caspase-7

详细信息	查看全文 | 推荐本文 |

• 作者：Taiki Nagano^a ; ^b ; Toshiaki Hashimoto^a ; Akio Nakashima^a ; Ushio Kikkawa^a ; ^b ; Shinji Kamada^a ; ^b ; ^{skamada@kobe-u.ac.jp}
• 关键词：IAPs ; inhibitor of apoptosis proteins ; BIR ; baculovirus IAP repeat ; XIAP ; X-linked inhibitor of apoptosis protein ; NEDD8 ; neural precursor cell expressed ; developmentally downregulated 8 ; GFP ; green fluorescent protein ; HA ; hemagglutinin
• 刊名：FEBS Letters
• 出版年：2012
• 期刊代码：70_00145793
• 类别：bio
• 出版时间：4 June, 2012
• 卷：586
• 期：11
• 页码：1612-1616
• 文件大小：533 K

摘要

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

with by ()

with by ()