ArticleCell death and differentiation2016
The initiator caspase Dronc is subject of enhanced autophagy upon proteasome impairment in Drosophila.
Article in Cell death and differentiation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Cytosolic mtDNA and associated EYA-mediated pro-inflammatory signaling modulate healthspan in Drosophila.Research square · 2025Article
- Accumulation of F-actin drives brain aging and limits healthspan in Drosophila.Nature communications · 2024Article
- Intrinsic apoptosis is evolutionarily divergent among metazoans.Evolution letters · 2024Article
- mTORC1 is required for differentiation of germline stem cells in the Drosophila melanogaster testis.PloS one · 2024Article
- Neuronal induction of BNIP3-mediated mitophagy slows systemic aging inNature aging · 2022Article
- A conserved myotubularin-related phosphatase regulates autophagy by maintaining autophagic flux.The Journal of cell biology · 2020Article
- Targeting intrinsic cell death pathways to control fungal pathogens.Biochemical pharmacology · 2019Review
- Plasma Membrane Localization of Apoptotic Caspases for Non-apoptotic Functions.Developmental cell · 2018Article
- Hsp83 loss suppresses proteasomal activity resulting in an upregulation of caspase-dependent compensatory autophagy.Autophagy · 2017Article
- Controlling caspase activity in life and death.PLoS genetics · 2017Article
- An inhibitory mono-ubiquitylation of the Drosophila initiator caspase Dronc functions in both apoptotic and non-apoptotic pathways.PLoS genetics · 2017Article
- Autophagy-independent function of Atg1 for apoptosis-induced compensatory proliferation.BMC biology · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
A major function of ubiquitylation is to deliver target proteins to the proteasome for degradation. In the apoptotic pathway in Drosophila, the inhibitor of apoptosis protein 1 (Diap1) regulates the activity of the initiator caspase Dronc (death regulator Nedd2-like caspase; caspase-9 ortholog) by ubiquitylation, supposedly targeting Dronc for degradation by the proteasome. Using a genetic approach, we show that Dronc protein fails to accumulate in epithelial cells with impaired proteasome function suggesting that it is not degraded by the proteasome, contrary to the expectation. Similarly, decreased autophagy, an alternative catabolic pathway, does not result in increased Dronc protein levels. However, combined impairment of the proteasome and autophagy triggers accumulation of Dronc protein levels suggesting that autophagy compensates for the loss of the proteasome with respect to Dronc turnover. Consistently, we show that loss of the proteasome enhances endogenous autophagy in epithelial cells. We propose that enhanced autophagy degrades Dronc if proteasome function is impaired.
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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.