{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["301(9)"],"submitter":["Juyoux P"],"pubmed_abstract":["Kinases are a diverse group of enzymes that use ATP to phosphorylate a variety of substrates. Protein kinases evolved in eukaryotes as important mediators of cell signaling that target specific amino acid side chains to modulate downstream protein function. Among them, the mitogen-activated protein kinases (MAPKs) are a family of intracellular protein kinases that form signaling cascades responding to a number of stimuli, which control fundamental mechanisms such as proliferation, differentiation, inflammation, and cell death. Signals propagate through consecutive kinases which eventually phosphorylate and activate a MAPK. Here, we show that the dual-specificity threonine/tyrosine mitogen-activated protein kinase kinases (MAP2Ks or MEKs) are able to phosphorylate and activate their substra"],"journal":["The Journal of biological chemistry"],"pagination":["110578"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12446509"],"repository":["biostudies-literature"],"pubmed_title":["Dual-specificity mitogen-activated protein kinase kinases can use ADP to phosphorylate MAP kinases invitro."],"pmcid":["PMC12446509"],"pubmed_authors":["Bowler MW","von Velsen J","Juyoux P","Pellegrini E"],"additional_accession":[]},"is_claimable":false,"name":"Dual-specificity mitogen-activated protein kinase kinases can use ADP to phosphorylate MAP kinases invitro.","description":"Kinases are a diverse group of enzymes that use ATP to phosphorylate a variety of substrates. Protein kinases evolved in eukaryotes as important mediators of cell signaling that target specific amino acid side chains to modulate downstream protein function. Among them, the mitogen-activated protein kinases (MAPKs) are a family of intracellular protein kinases that form signaling cascades responding to a number of stimuli, which control fundamental mechanisms such as proliferation, differentiation, inflammation, and cell death. Signals propagate through consecutive kinases which eventually phosphorylate and activate a MAPK. Here, we show that the dual-specificity threonine/tyrosine mitogen-activated protein kinase kinases (MAP2Ks or MEKs) are able to phosphorylate and activate their substra","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-06-03T15:24:19.533Z","creation":"2026-04-29T03:12:03.138Z"},"accession":"S-EPMC12446509","cross_references":{"pubmed":["40784449"],"doi":["10.1016/j.jbc.2025.110578"]}}