<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Rajagopal V</submitter><funding>Deutsche Forschungsgemeinschaft</funding><funding>Deutsche Forschungsgemeinschaft (German Research Foundation)</funding><funding>Deutsche Krebshilfe</funding><funding>Baden-Württemberg Stiftung (Baden-Württemberg Foundation)</funding><funding>Center for Strategic Scientific Initiatives, National Cancer Institute (NCI Center for Strategic Scientific Initiatives)</funding><funding>NCI NIH HHS</funding><funding>Baden-Württemberg Stiftung</funding><funding>U.S. Department of Health &amp; Human Services | National Institutes of Health (NIH)</funding><funding>Center for Strategic Scientific Initiatives, National Cancer Institute</funding><funding>NIGMS NIH HHS</funding><funding>U.S. Department of Health &amp;amp; Human Services | National Institutes of Health</funding><funding>Deutsche Krebshilfe (German Cancer Aid)</funding><pagination>2325</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11890761</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>16(1)</volume><pubmed_abstract>Ribonucleoprotein complexes are dynamic assemblies of RNA with RNA-binding proteins, which modulate the fate of RNA. Inversely, RNA riboregulates the interactions and functions of the associated proteins. Dysregulation of ribonucleoprotein functions is linked to diseases such as cancer and neurological disorders. In dividing cells, RNA and RNA-binding proteins are present in mitotic structures, but their impact on cell division remains unclear. By applying the proteome-wide R-DeeP strategy to cells synchronized in mitosis versus interphase integrated with the RBP2GO knowledge, we provided an atlas of RNA-dependent proteins in cell division, accessible at R-DeeP3.dkfz.de. We uncovered AURKA, KIFC1 and TPX2 as unconventional RNA-binding proteins. KIFC1 was identified as a new substrate of AU</pubmed_abstract><journal>Nature communications</journal><pubmed_title>An atlas of RNA-dependent proteins in cell division reveals the riboregulation of mitotic protein-protein interactions.</pubmed_title><pmcid>PMC11890761</pmcid><funding_grant_id>P30 CA023108</funding_grant_id><funding_grant_id>70113919</funding_grant_id><funding_grant_id>BWST-ISF2019-027</funding_grant_id><funding_grant_id>P30CA023108 DCC Core grant</funding_grant_id><funding_grant_id>R35 GM119455</funding_grant_id><funding_grant_id>DFG ZA 881/6-1 (project 541627224)</funding_grant_id><funding_grant_id>R35GM119455</funding_grant_id><pubmed_authors>Rajagopal V</pubmed_authors><pubmed_authors>Theiss J</pubmed_authors><pubmed_authors>Kettenbach AN</pubmed_authors><pubmed_authors>Seiler J</pubmed_authors><pubmed_authors>Cantarella S</pubmed_authors><pubmed_authors>Diederichs S</pubmed_authors><pubmed_authors>Herget F</pubmed_authors><pubmed_authors>Schneider M</pubmed_authors><pubmed_authors>Will R</pubmed_authors><pubmed_authors>Nasa I</pubmed_authors><pubmed_authors>Kaifer B</pubmed_authors><pubmed_authors>Konig J</pubmed_authors><pubmed_authors>Zarnack K</pubmed_authors><pubmed_authors>Caudron-Herger M</pubmed_authors><pubmed_authors>Klostermann M</pubmed_authors><pubmed_authors>Helm D</pubmed_authors></additional><is_claimable>false</is_claimable><name>An atlas of RNA-dependent proteins in cell division reveals the riboregulation of mitotic protein-protein interactions.</name><description>Ribonucleoprotein complexes are dynamic assemblies of RNA with RNA-binding proteins, which modulate the fate of RNA. Inversely, RNA riboregulates the interactions and functions of the associated proteins. Dysregulation of ribonucleoprotein functions is linked to diseases such as cancer and neurological disorders. In dividing cells, RNA and RNA-binding proteins are present in mitotic structures, but their impact on cell division remains unclear. By applying the proteome-wide R-DeeP strategy to cells synchronized in mitosis versus interphase integrated with the RBP2GO knowledge, we provided an atlas of RNA-dependent proteins in cell division, accessible at R-DeeP3.dkfz.de. We uncovered AURKA, KIFC1 and TPX2 as unconventional RNA-binding proteins. KIFC1 was identified as a new substrate of AU</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Mar</publication><modification>2026-06-01T20:12:16.511Z</modification><creation>2025-04-07T07:48:55.187Z</creation></dates><accession>S-EPMC11890761</accession><cross_references><pubmed>40057470</pubmed><doi>10.1038/s41467-025-57671-3</doi></cross_references></HashMap>