{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang L"],"funding":["NIGMS NIH HHS"],"pagination":["eabm8435"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8956257"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(12)"],"pubmed_abstract":["Phosphorylation can quickly switch on/off protein functions. Here, we reported pre-mRNA processing 4 kinase A (PRP4KA), and its paralogs interact with Serrate (SE), a key factor in RNA processing. PRP4KA phosphorylates at least five residues of SE in vitro and in vivo. Hypophosphorylated, but not hyperphosphorylated, SE variants could readily rescue <i>se</i> phenotypes in vivo. Moreover, hypophosphorylated SE variants had stronger binding affinity to microprocessor component HYL1 and were more resistant to degradation by 20<i>S</i> proteasome than hyperphosphorylated counterparts. Knockdown of the kinases enhanced the accumulation of hypophosphorylated SE. However, the excessive SE interfered with the assembly and function of SE-scaffolded macromolecule complexes, causing the <i>se</i>-li"],"journal":["Science advances"],"pubmed_title":["PRP4KA phosphorylates SERRATE for degradation via 20<i>S</i> proteasome to fine-tune miRNA production in <i>Arabidopsis</i>."],"pmcid":["PMC8956257"],"funding_grant_id":["R01 GM132401"],"pubmed_authors":["Shang B","Choi SW","Li Y","Zhang X","Chhajed S","Chen S","Yan X","Wang Z","Wang L","Zhao H"],"additional_accession":[]},"is_claimable":false,"name":"PRP4KA phosphorylates SERRATE for degradation via 20<i>S</i> proteasome to fine-tune miRNA production in <i>Arabidopsis</i>.","description":"Phosphorylation can quickly switch on/off protein functions. Here, we reported pre-mRNA processing 4 kinase A (PRP4KA), and its paralogs interact with Serrate (SE), a key factor in RNA processing. PRP4KA phosphorylates at least five residues of SE in vitro and in vivo. Hypophosphorylated, but not hyperphosphorylated, SE variants could readily rescue <i>se</i> phenotypes in vivo. Moreover, hypophosphorylated SE variants had stronger binding affinity to microprocessor component HYL1 and were more resistant to degradation by 20<i>S</i> proteasome than hyperphosphorylated counterparts. Knockdown of the kinases enhanced the accumulation of hypophosphorylated SE. However, the excessive SE interfered with the assembly and function of SE-scaffolded macromolecule complexes, causing the <i>se</i>-li","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2026-06-18T08:50:31.92Z","creation":"2025-04-19T20:12:41.027Z"},"accession":"S-EPMC8956257","cross_references":{"pubmed":["35333566"],"doi":["10.1126/sciadv.abm8435"]}}