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dc.contributor.authorMardakheh, FK
dc.contributor.authorSelf, A
dc.contributor.authorMarshall, CJ
dc.date.accessioned2018-06-06T11:27:18Z
dc.date.issued2016-12
dc.identifier.citationJournal of cell science, 2016, 129 (24), pp. 4466 - 4479
dc.identifier.issn0021-9533
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/1749
dc.identifier.eissn1477-9137
dc.identifier.doi10.1242/jcs.198614
dc.description.abstractDirectional cell migration involves reorientation of the secretory machinery. However, the molecular mechanisms that control this reorientation are not well characterised. Here, we identify a new Rho effector protein, named FAM65A, which binds to active RHOA, RHOB and RHOC. FAM65A links RHO proteins to Golgi-localising cerebral cavernous malformation-3 protein (CCM3; also known as PDCD10) and its interacting proteins mammalian STE20-like protein kinases 3 and 4 (MST3 and MST4; also known as STK24 and STK26, respectively). Binding of active RHO proteins to FAM65A does not affect the kinase activity of MSTs but results in their relocation from the Golgi in a CCM3-dependent manner. This relocation is crucial for reorientation of the Golgi towards the leading edge and subsequent directional cell migration. Our results reveal a previously unidentified pathway downstream of RHO that regulates the polarity of migrating cells through Golgi reorientation in a FAM65A-, CCM3- and MST3- and MST4-dependent manner.
dc.formatPrint-Electronic
dc.format.extent4466 - 4479
dc.languageeng
dc.language.isoeng
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.subjectHela Cells
dc.subjectGolgi Apparatus
dc.subjectHumans
dc.subjectrho GTP-Binding Proteins
dc.subjectProtein-Serine-Threonine Kinases
dc.subjectIntracellular Signaling Peptides and Proteins
dc.subjectMembrane Proteins
dc.subjectProto-Oncogene Proteins
dc.subjectCell Movement
dc.subjectEnzyme Activation
dc.subjectAmino Acid Sequence
dc.subjectProtein Binding
dc.subjectProtein Transport
dc.subjectApoptosis Regulatory Proteins
dc.titleRHO binding to FAM65A regulates Golgi reorientation during cell migration.
dc.typeJournal Article
dcterms.dateAccepted2016-10-24
rioxxterms.versionofrecord10.1242/jcs.198614
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.licenseref.startdate2016-12
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfJournal of cell science
pubs.issue24
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams/Oncogene
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams/Oncogene
pubs.publication-statusPublished
pubs.volume129
pubs.embargo.termsNot known
pubs.oa-locationhttp://jcs.biologists.org/content/joces/129/24/4466.full.pdf
icr.researchteamOncogeneen_US
dc.contributor.icrauthorMarshall, Christopheren


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