Invertebrate Survivin-like IAP Blocks Apoptosis

Science's STKE  25 Jul 2000:
Vol. 2000, Issue 42, pp. tw5
DOI: 10.1126/stke.2000.42.tw5

The process of apoptosis requires tight controls to prevent excessive cell death and aberrant proliferation. The inhibitors of apoptosis proteins (IAPs) block caspase activation, in addition to performing other recently discovered intracellular functions. Although IAPs typically contain several baculovirus IAP-like repeats (BIRs) and a RING finger domain, other IAPs--the Survivins--only contain one BIR and no RING finger. Survivin-type IAPs have been identified in mammals and Caenorhabditis elegans, but the invertebrate Survivin protein termed BIR1 only appears to have a role in cell division. Jones et al. describe the cloning and characterization of a Survivin-type IAP from Drosophila, termed Deterin, that has anti-apoptotic activity. Cells expressing dominant negative mutants or exhibiting RNA interference (RNAi) of Deterin succumbed to apoptosis. The effect of Deterin did not overlap with the anti-apoptotic activities of baculovirus p35 protein or Drosophila DIAP1, as measured by dominant-negative overexpression of Deterin, suggesting that each protein blocks apoptosis at different points. Thus, Deterin is the first invertebrate Survivin-type IAP family member to be identified that blocks apoptosis.

Jones, G., Jones, D., Zhou, L., Steller,H., and Chu, Y. Deterin, a new inhibitor of apoptosis from Drosophila melanogaster. J. Biol. Chem. 275: 22157-22165. [Abstract] [Full Text]