Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors.

We describe three mammalian homologs of inhibitor of apoptosis protein, MIHA, MIHB, and MIHC, and a Drosophila inhibitors of apoptosis homolog, DIHA

A. G. Uren; M. Pakusch; C. J. Hawkins; K. L. Puls; D. L. Vaux


Scholarcy highlights

  • Baculovirus inhibitors of apoptosis act in insect cells to prevent cell death
  • To see if there were other cellular IAP homologs and to determine if they function in cell death pathways, we undertook a search for genes encoding novel IAP proteins and tested their ability to inhibit apoptosis mediated by interleukin converting enzyme and by FADD
  • Libraries were screened with the probes to isolate cDNA clones, which we designated mammalian IAP homologs A, B, and C and Drosophila IAP homolog A
  • No interactions were detectable in this system between any of the TNF receptor-associated factor. Data deposition tested and Orgyia pseudotsugata nuclear polyhedrosis virus IAP or MIHA. These results show that MIHB and MIHC can bind to TRAFI and TRAF2, but suggest that OpIAP and MIHA interact with other proteins or that OpIAP and MIHA do not function in the yeast assays the same way as they do in mammalian cells
  • We have described three novel mammalian IAP proteins and an IAP homolog from Drosophila
  • This work was undertaken with the hope that study of viral IAPs and their cellular counterparts would reveal something about the less well-characterized stages of the cell death process
  • This suggests that TNF receptor-associated factor. Data deposition binding ability of inhibitor of apoptosis protein may not correlate with their anti-apoptotic activity, conditions in yeast may not accurately reflect conditions in mammalian cells

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