Myosin-18B Promotes the Assembly of Myosin II Stacks for Maturation of Contractile Actomyosin Bundles

Show simple item record

dc.contributor.author Jiu, Yaming
dc.contributor.author Kumari, Reena
dc.contributor.author Fenix, Aidan M.
dc.contributor.author Schaible, Niccole
dc.contributor.author Liu, Xiaonan
dc.contributor.author Varjosalo, Markku
dc.contributor.author Krishnan, Ramaswamy
dc.contributor.author Burnette, Dylan T.
dc.contributor.author Lappalainen, Pekka
dc.date.accessioned 2019-01-08T10:42:01Z
dc.date.available 2019-01-08T10:42:01Z
dc.date.issued 2019-01
dc.identifier.citation Jiu , Y , Kumari , R , Fenix , A M , Schaible , N , Liu , X , Varjosalo , M , Krishnan , R , Burnette , D T & Lappalainen , P 2019 , ' Myosin-18B Promotes the Assembly of Myosin II Stacks for Maturation of Contractile Actomyosin Bundles ' , Current Biology , vol. 29 , no. 1 , pp. 81-92 . https://doi.org/10.1016/j.cub.2018.11.045
dc.identifier.other PURE: 120793437
dc.identifier.other PURE UUID: db893ea9-910a-43df-9d13-fb925383a7d7
dc.identifier.other RIS: urn:D846CE608FB2862FAA42D0E3DED87C6B
dc.identifier.other ORCID: /0000-0002-1340-9732/work/52397918
dc.identifier.other Scopus: 85059557194
dc.identifier.other WOS: 000455224500023
dc.identifier.other ORCID: /0000-0001-9053-9461/work/82468985
dc.identifier.uri http://hdl.handle.net/10138/288205
dc.description.abstract Summary Cell adhesion, morphogenesis, mechanosensing, and muscle contraction rely on contractile actomyosin bundles, where the force is produced through sliding of bipolar myosin II filaments along actin filaments. The assembly of contractile actomyosin bundles involves registered alignment of myosin II filaments and their subsequent fusion into large stacks. However, mechanisms underlying the assembly of myosin II stacks and their physiological functions have remained elusive. Here, we identified myosin-18B, an unconventional myosin, as a stable component of contractile stress fibers. Myosin-18B co-localized with myosin II motor domains in stress fibers and was enriched at the ends of myosin II stacks. Importantly, myosin-18B deletion resulted in drastic defects in the concatenation and persistent association of myosin II filaments with each other and thus led to severely impaired assembly of myosin II stacks. Consequently, lack of myosin-18B resulted in defective maturation of actomyosin bundles from their precursors in osteosarcoma cells. Moreover, myosin-18B knockout cells displayed abnormal morphogenesis, migration, and ability to exert forces to the environment. These results reveal a critical role for myosin-18B in myosin II stack assembly and provide evidence that myosin II stacks are important for a variety of vital processes in cells. en
dc.format.extent 12
dc.language.iso eng
dc.relation.ispartof Current Biology
dc.rights cc_by_nc_nd
dc.rights.uri info:eu-repo/semantics/openAccess
dc.subject myosin-18B
dc.subject actin
dc.subject stress fiber
dc.subject actomyosin bundles
dc.subject myosin II
dc.subject cytoskeleton
dc.subject mechanosensing
dc.subject cell migration
dc.subject 1182 Biochemistry, cell and molecular biology
dc.title Myosin-18B Promotes the Assembly of Myosin II Stacks for Maturation of Contractile Actomyosin Bundles en
dc.type Article
dc.contributor.organization Staff Services
dc.contributor.organization Institute of Biotechnology
dc.contributor.organization Doctoral Programme in Integrative Life Science
dc.contributor.organization Doctoral Programme in Biomedicine
dc.contributor.organization Doctoral Programme in Drug Research
dc.contributor.organization University Management
dc.contributor.organization Molecular Systems Biology
dc.contributor.organization Pekka Lappalainen / Principal Investigator
dc.description.reviewstatus Peer reviewed
dc.relation.doi https://doi.org/10.1016/j.cub.2018.11.045
dc.relation.issn 0960-9822
dc.rights.accesslevel openAccess
dc.type.version draft

Files in this item

Total number of downloads: Loading...

Files Size Format View
1_s2.0_S0960982218315446_main.pdf 4.547Mb PDF View/Open

This item appears in the following Collection(s)

Show simple item record