A binding protein regulates myosin-7a dimerization and actin bundle assembly.
Nat Commun
; 12(1): 563, 2021 01 25.
Article
em En
| MEDLINE
| ID: mdl-33495456
ABSTRACT
Myosin-7a, despite being monomeric in isolation, plays roles in organizing actin-based cell protrusions such as filopodia, microvilli and stereocilia, as well as transporting cargoes within them. Here, we identify a binding protein for Drosophila myosin-7a termed M7BP, and describe how M7BP assembles myosin-7a into a motile complex that enables cargo translocation and actin cytoskeletal remodeling. M7BP binds to the autoinhibitory tail of myosin-7a, extending the molecule and activating its ATPase activity. Single-molecule reconstitution show that M7BP enables robust motility by complexing with myosin-7a as 22 translocation dimers in an actin-regulated manner. Meanwhile, M7BP tethers actin, enhancing complex's processivity and driving actin-filament alignment during processive runs. Finally, we show that myosin-7a-M7BP complex assembles actin bundles and filopodia-like protrusions while migrating along them in living cells. Together, these findings provide insights into the mechanisms by which myosin-7a functions in actin protrusions.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Citoesqueleto de Actina
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Proteínas de Transporte
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Actinas
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Proteínas de Drosophila
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Miosina VIIa
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article