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

Mariam H. Orme, Gianmaria Liccardi, Nina Moderau, Rebecca Feltham, Sidonie Wicky-John, Tencho Tenev, Lior Aram, Rebecca Wilson, Katiuscia Bianchi, Otto Morris, Celia Monteiro Domingues, David Robertson, Meghana Tare, Alexander Wepf, David Williams, Andreas Bergmann, Matthias Gstaiger, Eli Arama, Paulo S. Ribeiro and Pascal Meier ()
Additional contact information
Mariam H. Orme: Chester Beatty Laboratories, The Breast Cancer Now Toby Robins Research Centre, Institute of Cancer Research
Gianmaria Liccardi: Chester Beatty Laboratories, The Breast Cancer Now Toby Robins Research Centre, Institute of Cancer Research
Nina Moderau: John Vane Science Centre, Centre for Tumour Biology, Barts Cancer Institute, Queen Mary University of London, Charterhouse Square, London EC1M 6BQ, UK
Rebecca Feltham: Chester Beatty Laboratories, The Breast Cancer Now Toby Robins Research Centre, Institute of Cancer Research
Sidonie Wicky-John: Chester Beatty Laboratories, The Breast Cancer Now Toby Robins Research Centre, Institute of Cancer Research
Tencho Tenev: Chester Beatty Laboratories, The Breast Cancer Now Toby Robins Research Centre, Institute of Cancer Research
Lior Aram: Weizmann Institute of Science
Rebecca Wilson: Chester Beatty Laboratories, The Breast Cancer Now Toby Robins Research Centre, Institute of Cancer Research
Katiuscia Bianchi: Chester Beatty Laboratories, The Breast Cancer Now Toby Robins Research Centre, Institute of Cancer Research
Otto Morris: Chester Beatty Laboratories, The Breast Cancer Now Toby Robins Research Centre, Institute of Cancer Research
Celia Monteiro Domingues: Chester Beatty Laboratories, The Breast Cancer Now Toby Robins Research Centre, Institute of Cancer Research
David Robertson: Chester Beatty Laboratories, The Breast Cancer Now Toby Robins Research Centre, Institute of Cancer Research
Meghana Tare: University of Massachusetts Medical School
Alexander Wepf: ETH, Institute for Molecular Systems Biology
David Williams: UCLA David Geffen School of Medicine
Andreas Bergmann: University of Massachusetts Medical School
Matthias Gstaiger: ETH, Institute for Molecular Systems Biology
Eli Arama: Weizmann Institute of Science
Paulo S. Ribeiro: John Vane Science Centre, Centre for Tumour Biology, Barts Cancer Institute, Queen Mary University of London, Charterhouse Square, London EC1M 6BQ, UK
Pascal Meier: Chester Beatty Laboratories, The Breast Cancer Now Toby Robins Research Centre, Institute of Cancer Research

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms10972

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