Please use this identifier to cite or link to this item:
http://doi.org/10.25358/openscience-9348
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DC Field | Value | Language |
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dc.contributor.author | Bogucka-Janczi, Katarzyna | - |
dc.contributor.author | Harms, Gregory | - |
dc.contributor.author | Coissieux, Marie-May | - |
dc.contributor.author | Bentires-Alj, Mohamed | - |
dc.contributor.author | Thiede, Bernd | - |
dc.contributor.author | Rajalingam, Krishnaraj | - |
dc.date.accessioned | 2023-08-08T07:10:56Z | - |
dc.date.available | 2023-08-08T07:10:56Z | - |
dc.date.issued | 2023 | - |
dc.identifier.uri | https://openscience.ub.uni-mainz.de/handle/20.500.12030/9366 | - |
dc.description.abstract | The 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.sponsorship | Gefördert durch die Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 491381577 | de |
dc.language.iso | eng | de |
dc.rights | CC BY | * |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | * |
dc.subject.ddc | 610 Medizin | de_DE |
dc.subject.ddc | 610 Medical sciences | en_GB |
dc.title | ERK3/MAPK6 dictates CDC42/RAC1 activity and ARP2/3-dependent actin polymerization | en_GB |
dc.type | Zeitschriftenaufsatz | de |
dc.identifier.doi | http://doi.org/10.25358/openscience-9348 | - |
jgu.type.contenttype | Scientific article | de |
jgu.type.dinitype | article | en_GB |
jgu.type.version | Published version | de |
jgu.type.resource | Text | de |
jgu.organisation.department | FB 04 Medizin | de |
jgu.organisation.number | 2700 | - |
jgu.organisation.name | Johannes Gutenberg-Universität Mainz | - |
jgu.rights.accessrights | openAccess | - |
jgu.journal.title | eLife | de |
jgu.journal.volume | 12 | de |
jgu.pages.alternative | e85167 | de |
jgu.publisher.year | 2023 | - |
jgu.publisher.name | eLife Sciences Publications | de |
jgu.publisher.place | Cambridge | de |
jgu.publisher.issn | 2050-084X | de |
jgu.organisation.place | Mainz | - |
jgu.subject.ddccode | 610 | de |
jgu.publisher.doi | 10.7554/eLife.85167 | de |
jgu.organisation.ror | https://ror.org/023b0x485 | - |
jgu.subject.dfg | Naturwissenschaften | de |
Appears in collections: | DFG-491381577-G |
Files in This Item:
File | Description | Size | Format | ||
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erk3mapk6_dictates_cdc42rac1_-20230804114509889.pdf | 30.66 MB | Adobe PDF | View/Open |