dc.contributor.author | Orme, MH | |
dc.contributor.author | Liccardi, G | |
dc.contributor.author | Moderau, N | |
dc.contributor.author | Feltham, R | |
dc.contributor.author | Wicky-John, S | |
dc.contributor.author | Tenev, T | |
dc.contributor.author | Aram, L | |
dc.contributor.author | Wilson, R | |
dc.contributor.author | Bianchi, K | |
dc.contributor.author | Morris, O | |
dc.contributor.author | Monteiro Domingues, C | |
dc.contributor.author | Robertson, D | |
dc.contributor.author | Tare, M | |
dc.contributor.author | Wepf, A | |
dc.contributor.author | Williams, D | |
dc.contributor.author | Bergmann, A | |
dc.contributor.author | Gstaiger, M | |
dc.contributor.author | Arama, E | |
dc.contributor.author | Ribeiro, PS | |
dc.contributor.author | Meier, P | |
dc.date.accessioned | 2016-09-05T11:32:22Z | |
dc.date.issued | 2016-03-10 | |
dc.identifier.citation | Nature communications, 2016, 7 pp. 10972 - ? | |
dc.identifier.issn | 2041-1723 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/93 | |
dc.identifier.eissn | 2041-1723 | |
dc.identifier.doi | 10.1038/ncomms10972 | |
dc.description.abstract | 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. | |
dc.format | Electronic | |
dc.format.extent | 10972 - ? | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | NATURE PUBLISHING GROUP | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0 | |
dc.subject | Cell Line, Tumor | |
dc.subject | NIH 3T3 Cells | |
dc.subject | Animals | |
dc.subject | Humans | |
dc.subject | Mice | |
dc.subject | Drosophila melanogaster | |
dc.subject | Myosins | |
dc.subject | Caspases | |
dc.subject | Glycogen Synthase Kinase 3 | |
dc.subject | Drosophila Proteins | |
dc.subject | Microscopy, Confocal | |
dc.subject | Flow Cytometry | |
dc.subject | Immunoprecipitation | |
dc.subject | Signal Transduction | |
dc.subject | Caspase 8 | |
dc.subject | Receptor-Interacting Protein Serine-Threonine Kinases | |
dc.subject | Wings, Animal | |
dc.subject | Glycogen Synthase Kinase 3 beta | |
dc.subject | Myosin VIIa | |
dc.title | The unconventional myosin CRINKLED and its mammalian orthologue MYO7A regulate caspases in their signalling roles. | |
dc.type | Journal Article | |
dcterms.dateAccepted | 2016-02-05 | |
rioxxterms.versionofrecord | 10.1038/ncomms10972 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by/4.0 | |
rioxxterms.licenseref.startdate | 2016-03-10 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | Nature communications | |
pubs.notes | No embargo | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Breast Cancer Research | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Breast Cancer Research/Cell Death and Immunity | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Breast Cancer Research/Target Discovery & Apoptosis | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Therapeutics | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Therapeutics/Target Discovery & Apoptosis | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Breast Cancer Research | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Breast Cancer Research/Cell Death and Immunity | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Breast Cancer Research/Target Discovery & Apoptosis | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Therapeutics | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Cancer Therapeutics/Target Discovery & Apoptosis | |
pubs.publication-status | Published | |
pubs.volume | 7 | |
pubs.embargo.terms | No embargo | |
icr.researchteam | Cell Death and Immunity | |
icr.researchteam | Target Discovery & Apoptosis | |
dc.contributor.icrauthor | Morris, Otto | |
dc.contributor.icrauthor | Meier, Pascal | |