ArticleCell stress & chaperones2008
Hsp60D is essential for caspase-mediated induced apoptosis in Drosophila melanogaster.
Article in Cell stress & chaperones, 2008. 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, 19 citations in OpenAlex.
- Molecular Chaperonin HSP60: Current Understanding and Future Prospects.International journal of molecular sciences · 2024Review
- Zearalenone Does Not Show Genotoxic Effects in theToxins · 2023Article
- Mitochondria as a target and central hub of energy division during cold stress in insects.Frontiers in zoology · 2022Review
- Delayed discovery of Hsp60 and subsequent characterization of moonlighting functions of multipleJournal of genetics · 2022Article
- Expression status of heat shock proteins in response to cold, heat, or insecticide exposure in the Colorado potato beetle Leptinotarsa decemlineata.Cell stress & chaperones · 2019Article
- FUS Interacts with HSP60 to Promote Mitochondrial Damage.PLoS genetics · 2015Article
- Suppression of induced but not developmental apoptosis in Drosophila by Ayurvedic Amalaki Rasayana and Rasa-Sindoor.Journal of biosciences · 2015Article
- Neurodegeneration caused by polyglutamine expansion is regulated by P-glycoprotein in Drosophila melanogaster.Genetics · 2013Article
- Global transcriptome profiling of the pine shoot beetle, Tomicus yunnanensis (Coleoptera: Scolytinae).PloS one · 2012Article
- The heat shock proteins as targets for radiosensitization and chemosensitization in cancer.Cancer biology & therapy · 2011Review
- Modifiers and mechanisms of multi-system polyglutamine neurodegenerative disorders: lessons from fly models.Journal of genetics · 2010Review
- The developmentally active and stress-inducible noncoding hsromega gene is a novel regulator of apoptosis in Drosophila.Genetics · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Apart from their roles as chaperones, heat shock proteins are involved in other vital activities including apoptosis with mammalian Hsp60 being ascribed proapoptotic as well as antiapoptotic roles. Using conditional RNAi or overexpression of Hsp60D, a member of the Hsp60 family in Drosophila melanogaster, we show that the downregulation of this protein blocks caspase-dependent induced apoptosis. GMR-Gal4-driven RNAi for Hsp60D in developing eyes dominantly suppressed cell death caused by expression of Reaper, Hid, or Grim (RHG), the key activators of canonical cell death pathway. Likewise, Hsp60D-RNAi rescued cell death induced by GMR-Gal4-directed expression of full-length and activated DRONC. Overexpression of Hsp60D enhanced cell death induced either by directed expression of RHG or DRONC. However, the downregulation of Hsp60D failed to suppress apoptosis caused by unguarded caspases in DIAP1-RNAi flies. Furthermore, in DIAP1-RNAi background, Hsp60D-RNAi also failed to inhibit apoptosis induced by RHG expression. The Hsp60 and DIAP1 show diffuse and distinct granular overlapping distributions in the photoreceptor cells with the bulk of both proteins being outside the mitochondria. Depletion of either of these proteins disrupts the granular distribution of the other. We suggest that in the absence of Hsp60D, DIAP1 is unable to dissociate from effecter and executioner caspases, which thus remain inactive.
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