The unconventional myosin CRINKLED and its mammalian orthologue MYO7A regulate caspases in their signalling roles
UMass Chan Affiliations
Department of Molecular, Cell and Cancer BiologyDocument Type
Journal ArticlePublication Date
2016-03-10
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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-beta 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.Source
Nat Commun. 2016 Mar 10;7:10972. doi: 10.1038/ncomms10972. Link to article on publisher's siteDOI
10.1038/ncomms10972Permanent Link to this Item
http://hdl.handle.net/20.500.14038/40083PubMed ID
26960254Notes
Full author list omitted for brevity. For full list of authors see article.
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Link to Article in PubMedDistribution License
http://creativecommons.org/licenses/by/4.0/ae974a485f413a2113503eed53cd6c53
10.1038/ncomms10972
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Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by/4.0/