ArticleInsect molecular biology2009
A lepidopteran orthologue of reaper reveals functional conservation and evolution of IAP antagonists.
Article in Insect molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 63 citations in OpenAlex.
- Article
- Conceptual framework for the insect metamorphosis from larvae to pupae by transcriptomic profiling, a case study of Helicoverpa armigera (Lepidoptera: Noctuidae).BMC genomics · 2022Article
- Deep Conservation ofInsects · 2021Article
- Pro-Apoptotic Function Analysis of the Reaper Homologue IBM1 inInternational journal of molecular sciences · 2020Article
- Azadirachtin Affects the Growth ofFrontiers in physiology · 2018Article
- Article
- Mitochondrial Apoptotic Pathway Is Activated by H2O2-Mediated Oxidative Stress in BmN-SWU1 Cells from Bombyx mori Ovary.PloS one · 2015Article
- Screening of candidate proteins interacting with IE-2 of Bombyx mori nucleopolyhedrovirus.Molecular biology reports · 2013Article
- Multipolar functions of BCL-2 proteins link energetics to apoptosis.Trends in cell biology · 2012Review
- The role of IAP antagonist proteins in the core apoptosis pathway of the mosquito disease vector Aedes aegypti.Apoptosis : an international journal on programmed cell death · 2011Article
- The genomic underpinnings of apoptosis in the silkworm, Bombyx mori.BMC genomics · 2010Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Genetic studies in Drosophila melanogaster have revealed that inhibitor of apoptosis (IAP) proteins and IAP antagonists such as reaper play a pivotal role in controlling cell death in insects. Interestingly, although the sequences and structures of IAPs are highly conserved, the sequence of IAP antagonists diverged very rapidly during evolution, making their identification difficult. Using a customized bioinformatics approach, we identified an IAP antagonist, IAP-binding motif 1 (Ibm1), from the genome of the silkworm Bombyx mori. This is the first reaper/grim orthologue identified in a nondipteran insect. Previous analysis indicated that both Reaper and Grim induce cell death through their N-terminal IBM as well as the Grim_helix3 (GH3) domain. Functional studies indicated that Ibm1 binds to an IAP protein from B. mori, BmIAP1, and induces apoptosis in insect cells via the IAP-binding motif, a seven amino acid sequence that is highly conserved in all IAP antagonists. Interestingly, Ibm1 also contains a region that is a statistically significant match to the GH3 domain. Mutational analysis indicated that the GH3-like motif in Ibm1 has an important supportive role in IAP-antagonist function and can trigger cell death under certain conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.