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    The unconventional myosin CRINKLED and its mammalian orthologue MYO7A regulate caspases in their signalling roles.

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    Author
    Orme, MH; Liccardi, G; Moderau, N; Feltham, R; Wicky-John, S; Tenev, T; Aram, L; Wilson, R; Bianchi, K; Morris, O; ...
    Date
    2016-03-10
    Source Title
    Nature Communications
    Publisher
    Springer Science and Business Media LLC
    University of Melbourne Author/s
    Feltham, Rebecca
    Affiliation
    Medical Biology (W.E.H.I.)
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Orme, 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.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/253488
    DOI
    10.1038/ncomms10972
    Open Access at PMC
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4792956
    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.

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