Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-9348
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dc.contributor.authorBogucka-Janczi, Katarzyna-
dc.contributor.authorHarms, Gregory-
dc.contributor.authorCoissieux, Marie-May-
dc.contributor.authorBentires-Alj, Mohamed-
dc.contributor.authorThiede, Bernd-
dc.contributor.authorRajalingam, Krishnaraj-
dc.date.accessioned2023-08-08T07:10:56Z-
dc.date.available2023-08-08T07:10:56Z-
dc.date.issued2023-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/9366-
dc.description.abstractThe actin cytoskeleton is tightly controlled by RhoGTPases, actin binding-proteins and nucleation-promoting factors to perform fundamental cellular functions. We have previously shown that ERK3, an atypical MAPK, controls IL-8 production and chemotaxis (Bogueka et al., 2020). Here, we show in human cells that ERK3 directly acts as a guanine nucleotide exchange factor for CDC42 and phosphorylates the ARP3 subunit of the ARP2/3 complex at S418 to promote filopodia formation and actin polymerization, respectively. Consistently, depletion of ERK3 prevented both basal and EGF-dependent RAC1 and CDC42 activation, maintenance of F-actin content, filopodia formation, and epithelial cell migration. Further, ERK3 protein bound directly to the purified ARP2/3 complex and augmented polymerization of actin in vitro. ERK3 kinase activity was required for the formation of actin-rich protrusions in mammalian cells. These findings unveil a fundamentally unique pathway employed by cells to control actin-dependent cellular functions.en_GB
dc.description.sponsorshipGefördert durch die Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 491381577de
dc.language.isoengde
dc.rightsCC BY*
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subject.ddc610 Medizinde_DE
dc.subject.ddc610 Medical sciencesen_GB
dc.titleERK3/MAPK6 dictates CDC42/RAC1 activity and ARP2/3-dependent actin polymerizationen_GB
dc.typeZeitschriftenaufsatzde
dc.identifier.doihttp://doi.org/10.25358/openscience-9348-
jgu.type.contenttypeScientific articlede
jgu.type.dinitypearticleen_GB
jgu.type.versionPublished versionde
jgu.type.resourceTextde
jgu.organisation.departmentFB 04 Medizinde
jgu.organisation.number2700-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleeLifede
jgu.journal.volume12de
jgu.pages.alternativee85167de
jgu.publisher.year2023-
jgu.publisher.nameeLife Sciences Publicationsde
jgu.publisher.placeCambridgede
jgu.publisher.issn2050-084Xde
jgu.organisation.placeMainz-
jgu.subject.ddccode610de
jgu.publisher.doi10.7554/eLife.85167de
jgu.organisation.rorhttps://ror.org/023b0x485-
jgu.subject.dfgNaturwissenschaftende
Appears in collections:DFG-491381577-G

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