Structural and biochemical basis of apoptotic activation by Smac/DIABLO View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2000-08

AUTHORS

Jijie Chai, Chunying Du, Jia-Wei Wu, Saw Kyin, Xiaodong Wang, Yigong Shi

ABSTRACT

Apoptosis (programmed cell death), an essential process in the development and homeostasis of metazoans, is carried out by caspases. The mitochondrial protein Smac/DIABLO performs a critical function in apoptosis by eliminating the inhibitory effect of IAPs (inhibitor of apoptosis proteins) on caspases. Here we show that Smac/DIABLO promotes not only the proteolytic activation of procaspase-3 but also the enzymatic activity of mature caspase-3, both of which depend upon its ability to interact physically with IAPs. The crystal structure of Smac/DIABLO at 2.2 A resolution reveals that it homodimerizes through an extensive hydrophobic interface. Missense mutations inactivating this dimeric interface significantly compromise the function of Smac/DIABLO. As in the Drosophila proteins Reaper, Grim and Hid, the amino-terminal amino acids of Smac/DIABLO are indispensable for its function, and a seven-residue peptide derived from the amino terminus promotes procaspase-3 activation in vitro. These results establish an evolutionarily conserved structural and biochemical basis for the activation of apoptosis by Smac/DIABLO. More... »

PAGES

855

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/35022514

DOI

http://dx.doi.org/10.1038/35022514

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1051005104

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10972280


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