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Citation
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(): 10972.
FlyBase ID
FBrf0231258
Publication Type
Research paper
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.

PubMed ID
PubMed Central ID
PMC4792956 (PMC) (EuropePMC)
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Nat. Commun.
    Title
    Nature communications
    ISBN/ISSN
    2041-1723
    Data From Reference
    Genes (17)
    Physical Interactions (4)
    Cell Lines (1)