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dc.contributor.authorGreen, Hannah
dc.contributor.authorGriffiths, Annabel Gm
dc.contributor.authorYlänne, Jari
dc.contributor.authorBrown, Nicholas
dc.date.accessioned2018-11-05T10:24:49Z
dc.date.available2018-11-05T10:24:49Z
dc.date.issued2018-07-20
dc.identifier.issn2050-084X
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/284569
dc.description.abstractWe use the myotendinous junction of Drosophila flight muscles to explore why many integrin associated proteins (IAPs) are needed and how their function is coordinated. These muscles revealed new functions for IAPs not required for viability: Focal Adhesion Kinase (FAK), RSU1, tensin and vinculin. Genetic interactions demonstrated a balance between positive and negative activities, with vinculin and tensin positively regulating adhesion, while FAK inhibits elevation of integrin activity by tensin, and RSU1 keeps PINCH activity in check. The molecular composition of myofibril termini resolves into 4 distinct layers, one of which is built by a mechanotransduction cascade: vinculin facilitates mechanical opening of filamin, which works with the Arp2/3 activator WASH to build an actin-rich layer positioned between integrins and the first sarcomere. Thus, integration of IAP activity is needed to build the complex architecture of the myotendinous junction, linking the membrane anchor to the sarcomere.
dc.format.mediumElectronic
dc.languageeng
dc.publishereLife Sciences Publications, Ltd
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectMuscles
dc.subjectMyofibrils
dc.subjectSarcomeres
dc.subjectAnimals
dc.subjectDrosophila melanogaster
dc.subjectActins
dc.subjectVinculin
dc.subjectDrosophila Proteins
dc.subjectIntegrins
dc.subjectEpistasis, Genetic
dc.subjectRNA Interference
dc.subjectFlight, Animal
dc.subjectPhenotype
dc.subjectMutation
dc.titleNovel functions for integrin-associated proteins revealed by analysis of myofibril attachment in Drosophila.
dc.typeArticle
prism.publicationDate2018
prism.publicationNameElife
prism.volume7
dc.identifier.doi10.17863/CAM.31945
dcterms.dateAccepted2018-07-19
rioxxterms.versionofrecord10.7554/eLife.35783
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2018-07-20
dc.contributor.orcidGreen, Hannah [0000-0002-3039-3015]
dc.contributor.orcidYlänne, Jari [0000-0003-4627-021X]
dc.contributor.orcidBrown, Nicholas [0000-0002-8958-7017]
dc.identifier.eissn2050-084X
rioxxterms.typeJournal Article/Review
pubs.funder-project-idBiotechnology and Biological Sciences Research Council (BB/L006669/1)
pubs.funder-project-idWellcome Trust (099739/Z/12/Z)
cam.issuedOnline2018-07-20


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