dc.date.accessioned | 2024-01-20T18:37:02Z | |
dc.date.available | 2024-01-20T18:37:02Z | |
dc.date.created | 2023-06-21T14:21:29Z | |
dc.date.issued | 2023 | |
dc.identifier.citation | Bogucka-Janczi, Katarzyna Harms, Gregory Coissieux, Marie-May Bentires-Alj, Mohamed Thiede, Bernd Rajalingam, Krishnaraj . ERK3/MAPK6 dictates CDC42/RAC1 activity and ARP2/3-dependent actin polymerization. eLIFE. 2023, 12 | |
dc.identifier.uri | http://hdl.handle.net/10852/107101 | |
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. | |
dc.language | EN | |
dc.publisher | eLife Sciences Publications Ltd | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.title | ERK3/MAPK6 dictates CDC42/RAC1 activity and ARP2/3-dependent actin polymerization | |
dc.title.alternative | ENEngelskEnglishERK3/MAPK6 dictates CDC42/RAC1 activity and ARP2/3-dependent actin polymerization | |
dc.type | Journal article | |
dc.creator.author | Bogucka-Janczi, Katarzyna | |
dc.creator.author | Harms, Gregory | |
dc.creator.author | Coissieux, Marie-May | |
dc.creator.author | Bentires-Alj, Mohamed | |
dc.creator.author | Thiede, Bernd | |
dc.creator.author | Rajalingam, Krishnaraj | |
cristin.unitcode | 185,15,29,40 | |
cristin.unitname | Seksjon for biokjemi og molekylærbiologi | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 2 | |
dc.identifier.cristin | 2156671 | |
dc.identifier.bibliographiccitation | info:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=eLIFE&rft.volume=12&rft.spage=&rft.date=2023 | |
dc.identifier.jtitle | eLIFE | |
dc.identifier.volume | 12 | |
dc.identifier.pagecount | 0 | |
dc.identifier.doi | https://doi.org/10.7554/eLife.85167 | |
dc.type.document | Tidsskriftartikkel | |
dc.type.peerreviewed | Peer reviewed | |
dc.source.issn | 2050-084X | |
dc.type.version | PublishedVersion | |
cristin.articleid | e85167 | |