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dc.contributor.authorDobramysl, Ulrich
dc.contributor.authorJarsch, Iris Katharina
dc.contributor.authorInoue, Yoshiko
dc.contributor.authorShimo, Hanae
dc.contributor.authorRichier, Benjamin
dc.contributor.authorGadsby, Jonathan R
dc.contributor.authorMason, Julia
dc.contributor.authorSzałapak, Alicja
dc.contributor.authorIoannou, Pantelis Savvas
dc.contributor.authorCorreia, Guilherme Pereira
dc.contributor.authorWalrant, Astrid
dc.contributor.authorButler, Richard
dc.contributor.authorHannezo, Edouard
dc.contributor.authorSimons, Benjamin D
dc.contributor.authorGallop, Jennifer L
dc.date.accessioned2021-03-20T00:30:24Z
dc.date.available2021-03-20T00:30:24Z
dc.date.issued2021-04-05
dc.identifier.issn0021-9525
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/319010
dc.description.abstractAssemblies of actin and its regulators underlie the dynamic morphology of all eukaryotic cells. To understand how actin regulatory proteins work together to generate actin-rich structures such as filopodia, we analyzed the localization of diverse actin regulators within filopodia in Drosophila embryos and in a complementary in vitro system of filopodia-like structures (FLSs). We found that the composition of the regulatory protein complex where actin is incorporated (the filopodial tip complex) is remarkably heterogeneous both in vivo and in vitro. Our data reveal that different pairs of proteins correlate with each other and with actin bundle length, suggesting the presence of functional subcomplexes. This is consistent with a theoretical framework where three or more redundant subcomplexes join the tip complex stochastically, with any two being sufficient to drive filopodia formation. We provide an explanation for the observed heterogeneity and suggest that a mechanism based on multiple components allows stereotypical filopodial dynamics to arise from diverse upstream signaling pathways.
dc.description.sponsorshipHerchel Smith Fellowship, Funai Foundation scholarship, Austrian Science Fund
dc.format.mediumPrint
dc.languageeng
dc.publisherRockefeller University Press
dc.rightsAttribution 4.0 International (CC BY)
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectPseudopodia
dc.subjectEmbryo, Nonmammalian
dc.subjectAnimals
dc.subjectXenopus
dc.subjectDrosophila melanogaster
dc.subjectXenopus Proteins
dc.subjectDrosophila Proteins
dc.subjectFatty Acid-Binding Proteins
dc.titleStochastic combinations of actin regulatory proteins are sufficient to drive filopodia formation.
dc.typeArticle
prism.issueIdentifier4
prism.publicationDate2021
prism.publicationNameJ Cell Biol
prism.volume220
dc.identifier.doi10.17863/CAM.66129
dcterms.dateAccepted2021-01-12
rioxxterms.versionofrecord10.1083/jcb.202003052
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2021-04
dc.contributor.orcidDobramysl, Ulrich [0000-0001-9363-654X]
dc.contributor.orcidGadsby, Jonathan [0000-0001-7986-4917]
dc.contributor.orcidButler, Richard [0000-0002-3885-1332]
dc.contributor.orcidSimons, Benjamin [0000-0002-3875-7071]
dc.contributor.orcidGallop, Jennifer [0000-0002-9978-1382]
dc.identifier.eissn1540-8140
rioxxterms.typeJournal Article/Review
pubs.funder-project-idWellcome Trust (095829/Z/11/Z)
pubs.funder-project-idEuropean Research Council (281971)
pubs.funder-project-idWellcome Trust (219482/Z/19/Z)
pubs.funder-project-idWellcome Trust (092096/Z/10/Z)
pubs.funder-project-idCancer Research Uk (None)
pubs.funder-project-idWellcome Trust (098357/Z/12/Z)
pubs.funder-project-idWellcome Trust (105602/Z/14/Z)
pubs.funder-project-idMedical Research Council (MC_PC_17230)
cam.issuedOnline2021-03-19
cam.orpheus.successMon Mar 29 07:30:31 BST 2021 - The item has an open VoR version.
rioxxterms.freetoread.startdate2100-01-01


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Attribution 4.0 International (CC BY)
Except where otherwise noted, this item's licence is described as Attribution 4.0 International (CC BY)