Inhibition of reaper-induced apoptosis by interaction with inhibitor of apoptosis proteins (IAPs)

Domagoj Vucic, William J. Kaiser, Alex J. Harvey, Lois K. Miller

Research output: Contribution to journalArticlepeer-review

186 Scopus citations

Abstract

IAPs comprise a family of inhibitors of apoptosis found in viruses and animals. In vivo binding studies demonstrated that both baculovirus and Drosophila IAPs physically interact with an apoptosis-inducing protein of Drosophila, Reaper (RPR), through their baculovirus IAP repeat (BIR) region. Expression of IAPs blocked RPR-induced apoptosis and resulted in the accumulation of RPR in punctate perinuclear locations which coincided with IAP localization. When expressed alone, RPR rapidly disappeared from the cells undergoing RPR-induced apoptosis. Expression of P35, a caspase inhibitor, also blocked RPR-induced apoptosis and delayed RPR decline, but RPR remained cytoplasmic in its location. Mutational analysis of RPR demonstrated that caspases were not directly responsible for RPR disappearance. The physical interaction of IAPs with RPR provides a molecular mechanism for IAP inhibition of RPR's apoptotic activity.

Original languageEnglish (US)
Pages (from-to)10183-10188
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number19
DOIs
StatePublished - Sep 16 1997

ASJC Scopus subject areas

  • General

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