{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lizcano-Perret B"],"funding":["Fonds pour la Formation à la Recherche dans l’Industrie et dans l’Agriculture","EOS","Fonds De La Recherche Scientifique - FNRS","Actions de Recherches Concertées","Loterie Nationale"],"pagination":["e1011042"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9779665"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(12)"],"pubmed_abstract":["Proteins from some unrelated pathogens, including small RNA viruses of the family Picornaviridae, large DNA viruses such as Kaposi sarcoma-associated herpesvirus and even bacteria of the genus Yersinia can recruit cellular p90-ribosomal protein S6 kinases (RSKs) through a common linear motif and maintain the kinases in an active state. On the one hand, pathogens' proteins might hijack RSKs to promote their own phosphorylation (direct target model). On the other hand, some data suggested that pathogens' proteins might dock the hijacked RSKs toward a third interacting partner, thus redirecting the kinase toward a specific substrate. We explored the second hypothesis using the Cardiovirus leader protein (L) as a paradigm. The L protein is known to trigger nucleocytoplasmic trafficking perturb"],"journal":["PLoS pathogens"],"pubmed_title":["Cardiovirus leader proteins retarget RSK kinases toward alternative substrates to perturb nucleocytoplasmic traffic."],"pmcid":["PMC9779665"],"funding_grant_id":["ARC","PDR T.0185.14","grant via de Duve Institute","EOS ID: 30981113 and 40007527","fellowship"],"pubmed_authors":["Sorgeloos F","Hauchamps P","Wavreil F","Lizcano-Perret B","Lardinois C","Gatto L","Vertommen D","Herinckx G","Michiels T"],"additional_accession":[]},"is_claimable":false,"name":"Cardiovirus leader proteins retarget RSK kinases toward alternative substrates to perturb nucleocytoplasmic traffic.","description":"Proteins from some unrelated pathogens, including small RNA viruses of the family Picornaviridae, large DNA viruses such as Kaposi sarcoma-associated herpesvirus and even bacteria of the genus Yersinia can recruit cellular p90-ribosomal protein S6 kinases (RSKs) through a common linear motif and maintain the kinases in an active state. On the one hand, pathogens' proteins might hijack RSKs to promote their own phosphorylation (direct target model). On the other hand, some data suggested that pathogens' proteins might dock the hijacked RSKs toward a third interacting partner, thus redirecting the kinase toward a specific substrate. We explored the second hypothesis using the Cardiovirus leader protein (L) as a paradigm. The L protein is known to trigger nucleocytoplasmic trafficking perturb","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-05-29T19:00:10.299Z","creation":"2024-11-10T02:21:32.593Z"},"accession":"S-EPMC9779665","cross_references":{"pubmed":["36508477"],"doi":["10.1371/journal.ppat.1011042"]}}