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However, only a few DYRK1B substrates have been defined, so we undertook a phosphoproteomics screen in cells that exhibit inducible DYRK1B expression. Motif analysis revealed enrichment for proline-directed serine or threonine phosphorylation sites (pSer\u2013Pro or pThr\u2013Pro), consistent with the consensus motif of class I DYRKs. Gene Ontology (GO) analysis revealed enrichment of proteins involved in mRNA binding, mRNA processing and ribonucleoprotein complexes. Several processing body (PB) components, including DCP1A, PATL1 (PAT1B), EDC3 and 4E-T (also known as EIF4ENIF1), were identified as DYRK1B-inducible phosphoproteins. DYRK1B also co-immunoprecipitated with DCP1A, PAT1B, EDC3, EDC4, DDX6 and XRN1. Super-resolution microscopy demonstrated that DYRK1B co-localised with DCP1A, DCP1B and DDX6 in PBs. Expression of DYRK1B increased PB abundance, whereas inhibition, depletion or knockout of DYRK1B reduced phosphorylation of DCP1A and 4E-T and decreased PB number. Re-expression of wild-type but not kinase-dead DYRK1B restored PB numbers in knockout cells. These findings reveal novel DYRK1B targets and establish DYRK1B as a regulator of PB abundance.<\/jats:p>","DOI":"10.1242\/jcs.265054","type":"journal-article","created":{"date-parts":[[2026,8,13]],"date-time":"2026-08-13T09:55:51Z","timestamp":1786614951000},"source":"Crossref","is-referenced-by-count":0,"title":["Phosphoproteomics identifies the DYRK1B protein kinase as a regulator of processing bodies"],"prefix":"10.1242","volume":"139","author":[{"given":"Anne L.","family":"Ashford","sequence":"first","affiliation":[{"name":"The Babraham Institute 1 Signalling Programme , , Babraham Research Campus, Cambridge CB22 3AT ,","place":["UK"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4219-6032","authenticated-orcid":false,"given":"Suzan","family":"Ber","sequence":"additional","affiliation":[{"name":"The Babraham Institute 1 Signalling Programme , , Babraham Research Campus, Cambridge CB22 3AT 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