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dc.contributor.authorOrme, MH
dc.contributor.authorLiccardi, G
dc.contributor.authorModerau, N
dc.contributor.authorFeltham, R
dc.contributor.authorWicky-John, S
dc.contributor.authorTenev, T
dc.contributor.authorAram, L
dc.contributor.authorWilson, R
dc.contributor.authorBianchi, K
dc.contributor.authorMorris, O
dc.contributor.authorMonteiro Domingues, C
dc.contributor.authorRobertson, D
dc.contributor.authorTare, M
dc.contributor.authorWepf, A
dc.contributor.authorWilliams, D
dc.contributor.authorBergmann, A
dc.contributor.authorGstaiger, M
dc.contributor.authorArama, E
dc.contributor.authorRibeiro, PS
dc.contributor.authorMeier, P
dc.date.accessioned2020-12-10T00:25:52Z
dc.date.available2020-12-10T00:25:52Z
dc.date.issued2016-03-10
dc.identifierpii: ncomms10972
dc.identifier.citationOrme, M. H., Liccardi, G., Moderau, N., Feltham, R., Wicky-John, S., Tenev, T., Aram, L., Wilson, R., Bianchi, K., Morris, O., Monteiro Domingues, C., Robertson, D., Tare, M., Wepf, A., Williams, D., Bergmann, A., Gstaiger, M., Arama, E., Ribeiro, P. S. & Meier, P. (2016). The unconventional myosin CRINKLED and its mammalian orthologue MYO7A regulate caspases in their signalling roles.. Nat Commun, 7 (1), pp.10972-. https://doi.org/10.1038/ncomms10972.
dc.identifier.issn2041-1723
dc.identifier.urihttp://hdl.handle.net/11343/253488
dc.description.abstractCaspases 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.languageeng
dc.publisherSpringer Science and Business Media LLC
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleThe unconventional myosin CRINKLED and its mammalian orthologue MYO7A regulate caspases in their signalling roles.
dc.typeJournal Article
dc.identifier.doi10.1038/ncomms10972
melbourne.affiliation.departmentMedical Biology (W.E.H.I.)
melbourne.source.titleNature Communications
melbourne.source.volume7
melbourne.source.issue1
melbourne.source.pages10972-
dc.rights.licenseCC BY
melbourne.elementsid1317881
melbourne.openaccess.pmchttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4792956
melbourne.contributor.authorFeltham, Rebecca
dc.identifier.eissn2041-1723
melbourne.accessrightsOpen Access


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