Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-11

AUTHORS

Jijie Chai, Nieng Yan, Jun R Huh, Jia-Wei Wu, Wenyu Li, Bruce A Hay, Yigong Shi

ABSTRACT

The inhibitor of apoptosis protein DIAP1 inhibits Dronc-dependent cell death by ubiquitinating Dronc. The pro-death proteins Reaper, Hid and Grim (RHG) promote apoptosis by antagonizing DIAP1 function. Here we report the structural basis of Dronc recognition by DIAP1 as well as a novel mechanism by which the RHG proteins remove DIAP1-mediated downregulation of Dronc. Biochemical and structural analyses revealed that the second BIR (BIR2) domain of DIAP1 recognizes a 12-residue sequence in Dronc. This recognition is essential for DIAP1 binding to Dronc, and for targeting Dronc for ubiquitination. Notably, the Dronc-binding surface on BIR2 coincides with that required for binding to the N termini of the RHG proteins, which competitively eliminate DIAP1-mediated ubiquitination of Dronc. These observations reveal the molecular mechanisms of how DIAP1 recognizes Dronc, and more importantly, how the RHG proteins remove DIAP1-mediated ubiquitination of Dronc. More... »

PAGES

892-898

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nsb989

    DOI

    http://dx.doi.org/10.1038/nsb989

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1013723082

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/14517550


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