{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Taylor CA"],"funding":["U.S. Department of Health & Human Services | NIH | National Cancer Institute (NCI)","Cancer Prevention and Research Institute of Texas (Cancer Prevention Research Institute of Texas)","NIA NIH HHS","U.S. Department of Health & Human Services | NIH | National Cancer Institute","NHLBI NIH HHS","NCI NIH HHS","Welch Foundation","Cancer Prevention and Research Institute of Texas"],"pagination":["1335"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12413468"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(1)"],"pubmed_abstract":["The WNK-OSR1/SPAK protein kinase pathway regulates ion homeostasis and cell volume, but its other functions are not well understood. To discover undefined signaling functions, we utilized experimentally-derived binding specificity to predict interactions and relative affinities with the conserved C-terminal (CCT) domains of OSR1 and SPAK, which bind short linear motifs. The upstream kinases WNKs 1-4 and their relatives, the pseudokinases NRBP1/2, also contain CCT-like domains which have conserved folds and motif binding pockets. Motifs were scored using peptide arrays, conservation, cytosolic localization, and solvent accessibility. Out of nearly 3700 motifs in the human proteome, 90% of previously published motifs ranked in the top 2% of those predicted. Interactions with selected candida"],"journal":["Communications biology"],"pubmed_title":["Kinase interaction analysis predicts actions of the WNK-OSR1/SPAK pathway."],"pmcid":["PMC12413468"],"funding_grant_id":["I1243","P30CA142543","RP210041","K99 AG075161","R01 HL147661","P30 CA142543"],"pubmed_authors":["Sauceda E","Cobb MH","Li J","Jaykumar AB","Earnest S","Jung JU","Stippec S","Grzemska M","Gallolu Kankanamalage S","Saha P","Taylor CA"],"additional_accession":[]},"is_claimable":false,"name":"Kinase interaction analysis predicts actions of the WNK-OSR1/SPAK pathway.","description":"The WNK-OSR1/SPAK protein kinase pathway regulates ion homeostasis and cell volume, but its other functions are not well understood. To discover undefined signaling functions, we utilized experimentally-derived binding specificity to predict interactions and relative affinities with the conserved C-terminal (CCT) domains of OSR1 and SPAK, which bind short linear motifs. The upstream kinases WNKs 1-4 and their relatives, the pseudokinases NRBP1/2, also contain CCT-like domains which have conserved folds and motif binding pockets. Motifs were scored using peptide arrays, conservation, cytosolic localization, and solvent accessibility. Out of nearly 3700 motifs in the human proteome, 90% of previously published motifs ranked in the top 2% of those predicted. Interactions with selected candida","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-06-03T02:16:28.05Z","creation":"2026-04-23T03:09:37.484Z"},"accession":"S-EPMC12413468","cross_references":{"pubmed":["40913030"],"doi":["10.1038/s42003-025-08551-5"]}}