@article{168451,
  keywords = {Animals, Molecular Sequence Data, Protein Binding, Amino Acid Sequence, Peptides, Drosophila melanogaster, Drosophila Proteins, Apoptosis, Ubiquitin, Inhibitor of Apoptosis Proteins, Caspases, Neuropeptides},
  author = {Jijie Chai and Nieng Yan and Jun Huh and Jia-Wei Wu and Wenyu Li and Bruce Hay and Yigong Shi},
  title = {Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination},
  abstract = {<p>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.</p>
},
  year = {2003},
  journal = {Nat Struct Biol},
  volume = {10},
  pages = {892-8},
  month = {11/2003},
  issn = {1072-8368},
  doi = {10.1038/nsb989},
  language = {eng},
}