Research ArticleCell death

Unique BIR domain sets determine inhibitor of apoptosis protein–driven cell death and NOD2 complex signal specificity

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Science Signaling  17 Jul 2018:
Vol. 11, Issue 539, eaao3964
DOI: 10.1126/scisignal.aao3964

Structure-function specificity of IAP proteins

Inhibitor of apoptosis proteins (IAPs) are involved in regulating cell death and inflammation. As such, both gain and loss of IAP function are associated with various diseases, from cancer to immune disorders. Chirieleison et al. examined the functional redundancy and selectivity of IAP family members as conferred by their structural motifs. The authors found that at least one IAP protein was critical for cell survival and that the catalytic domain of each protein, which provides E3 ubiquitin ligase activity, is redundant among the proteins but that its positioning within a triplet of protein-protein interaction domains confers distinct signaling functions among the proteins. These findings have implications for drug development as well as our understanding of the pathogenesis of immune disorders caused by IAP loss.

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