Bifunctional killing activity encoded by conserved reaper proteins

P. Chen, S. I. Ho, Z. Shi, John M. Abrams

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Drosophila activators of apoptosis mapping to the Reaper region function, in part, by antagonizing IAP proteins through a shared RHG motif. We isolated Reaper from the Blowfly L. cuprina, which triggered extensive apoptosis in Drosophila cells. Conserved regions of Reaper were tested in the context of GFP fusions and a second killing activity, distinct from the RHG, was identified. A 20 amino-acid peptide, designated R3, conferred targeting to a focal compartment and promoted membrane blebbing. Killing by the R3 fragment did not correlate with translational suppression or with reduced DIAP1 levels. Likewise, R3-induced cell deaths were only modestly suppressed by silencing of Dronc and involved no detectable association with DIAP1. Instead, a second IAP-binding domain, distinct from the R3, was identified at the C terminus of Reaper that bound to DIAP1 but failed to trigger apoptosis. Collectively, these findings are inconsistent with single effector models for cell killing by Reaper and suggest, instead, that Reaper encodes conserved bifunctional death activities that propagate through distinct effector pathways.

Original languageEnglish (US)
Pages (from-to)704-713
Number of pages10
JournalCell Death and Differentiation
Volume11
Issue number7
DOIs
StatePublished - Jul 2004

Fingerprint

Apoptosis
Drosophila
Proteins
Blister
Cell Death
Amino Acids
Peptides
Membranes

Keywords

  • Apoptosis
  • Caspases
  • Drosophila
  • IAP
  • Reaper

ASJC Scopus subject areas

  • Cell Biology

Cite this

Bifunctional killing activity encoded by conserved reaper proteins. / Chen, P.; Ho, S. I.; Shi, Z.; Abrams, John M.

In: Cell Death and Differentiation, Vol. 11, No. 7, 07.2004, p. 704-713.

Research output: Contribution to journalArticle

Chen, P. ; Ho, S. I. ; Shi, Z. ; Abrams, John M. / Bifunctional killing activity encoded by conserved reaper proteins. In: Cell Death and Differentiation. 2004 ; Vol. 11, No. 7. pp. 704-713.
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