{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sridharan S"],"funding":["European Research Council"],"pagination":["1104-1114"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9512703"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(10)"],"pubmed_abstract":["Reversible protein phosphorylation is an important mechanism for regulating (dis)assembly of biomolecular condensates. However, condensate-specific phosphosites remain largely unknown, thereby limiting our understanding of the underlying mechanisms. Here, we combine solubility proteome profiling with phosphoproteomics to quantitatively map several hundred phosphosites enriched in either soluble or condensate-bound protein subpopulations, including a subset of phosphosites modulating protein-RNA interactions. We show that multi-phosphorylation of the C-terminal disordered segment of heteronuclear ribonucleoprotein A1 (HNRNPA1), a key RNA-splicing factor, reduces its ability to locate to nuclear clusters. For nucleophosmin 1 (NPM1), an essential nucleolar protein, we show that phosphorylatio"],"journal":["Nature chemical biology"],"pubmed_title":["Systematic discovery of biomolecular condensate-specific protein phosphorylation."],"pmcid":["PMC9512703"],"funding_grant_id":["810296"],"pubmed_authors":["Hernandez-Armendariz A","Bantscheff M","Memon D","Huber W","Savitski MM","Beltrao P","Potel CM","Sridharan S","Kurzawa N","Cuylen-Haering S"],"additional_accession":[]},"is_claimable":false,"name":"Systematic discovery of biomolecular condensate-specific protein phosphorylation.","description":"Reversible protein phosphorylation is an important mechanism for regulating (dis)assembly of biomolecular condensates. However, condensate-specific phosphosites remain largely unknown, thereby limiting our understanding of the underlying mechanisms. Here, we combine solubility proteome profiling with phosphoproteomics to quantitatively map several hundred phosphosites enriched in either soluble or condensate-bound protein subpopulations, including a subset of phosphosites modulating protein-RNA interactions. We show that multi-phosphorylation of the C-terminal disordered segment of heteronuclear ribonucleoprotein A1 (HNRNPA1), a key RNA-splicing factor, reduces its ability to locate to nuclear clusters. For nucleophosmin 1 (NPM1), an essential nucleolar protein, we show that phosphorylatio","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2025-04-26T22:05:58.68Z","creation":"2025-04-06T17:03:43.586Z"},"accession":"S-EPMC9512703","cross_references":{"pubmed":["35864335"],"doi":["10.1038/s41589-022-01062-y"]}}