The unconventional myosin CRINKLED and its mammalian orthologue MYO7A regulate caspases in their signalling roles
| العنوان: | The unconventional myosin CRINKLED and its mammalian orthologue MYO7A regulate caspases in their signalling roles |
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| المؤلفون: | Orme, Mariam H., Liccardi, Gianmaria, Moderau, Nina, Feltham, Rebecca, Wicky-John, Sidonie, Tenev, Tencho, Aram, Lior, Wilson, Rebecca, Bianchi, Katiuscia, Morris, Otto, Monteiro Domingues, Celia, Robertson, David, Tare, Meghana, Wepf, Alexander, Williams, David, Bergmann, Andreas, Gstaiger, Matthias, Arama, Eli, Ribeiro, Paulo S., Meier, Pascal |
| المصدر: | Nature Communications Nature Communications, 7 Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016) |
| سنة النشر: | 2015 |
| مصطلحات موضوعية: | animal structures, DROSOPHILA-REAPER, Science, USHER PROTEINS, Myosins, Article, PROGRAMMED CELL-DEATH, ACTIVATION, Glycogen Synthase Kinase 3, Mice, Cell Line, Tumor, MD Multidisciplinary, Animals, Drosophila Proteins, Humans, Immunoprecipitation, Wings, Animal, HID, TUMOR-NECROSIS-FACTOR, DRONC, Caspase 8, Science & Technology, Glycogen Synthase Kinase 3 beta, Microscopy, Confocal, Flow Cytometry, TNF-ALPHA, GENE, APOPTOSIS, Multidisciplinary Sciences, Drosophila melanogaster, Caspases, Myosin VIIa, Receptor-Interacting Protein Serine-Threonine Kinases, NIH 3T3 Cells, Science & Technology - Other Topics, Signal Transduction |
| الوصف: | Caspases provide vital links in non-apoptotic regulatory networks controlling inflammation, compensatory proliferation, morphology and cell migration. How caspases are activated under non-apoptotic conditions and process a selective set of substrates without killing the cell remain enigmatic. Here we find that the Drosophila unconventional myosin CRINKLED (CK) selectively interacts with the initiator caspase DRONC and regulates some of its non-apoptotic functions. Loss of CK in the arista, border cells or proneural clusters of the wing imaginal discs affects DRONC-dependent patterning. Our data indicate that CK acts as substrate adaptor, recruiting SHAGGY46/GSK3-β to DRONC, thereby facilitating caspase-mediated cleavage and localized modulation of kinase activity. Similarly, the mammalian CK counterpart, MYO7A, binds to and impinges on CASPASE-8, revealing a new regulatory axis affecting receptor interacting protein kinase-1 (RIPK1)>CASPASE-8 signalling. Together, our results expose a conserved role for unconventional myosins in transducing caspase-dependent regulation of kinases, allowing them to take part in specific signalling events. Nature Communications, 7 ISSN:2041-1723 |
| وصف الملف: | application/application/pdf |
| تدمد: | 2041-1723 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::951ac484992446f9e079c83454f855d1 https://pubmed.ncbi.nlm.nih.gov/26960254 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....951ac484992446f9e079c83454f855d1 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 20411723 |
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