<HashMap><database>biostudies-literature</database><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>60</viewCount><searchCount>0</searchCount></scores><additional><submitter>Protter DSW</submitter><funding>T32</funding><funding>Howard Hughes Medical Institute</funding><funding>Welch Foundation</funding><funding>NIH</funding><funding>NIGMS NIH HHS</funding><pagination>1401-1412</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5824733</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>22(6)</volume><pubmed_abstract>Eukaryotic cells contain large RNA-protein assemblies referred to as RNP granules, whose assembly is promoted by both traditional protein interactions and intrinsically disordered protein domains. Using RNP granules as an example, we provide evidence for an assembly mechanism of large cellular structures wherein specific protein-protein or protein-RNA interactions act together with promiscuous interactions of intrinsically disordered regions (IDRs). This synergistic assembly mechanism illuminates RNP granule assembly and explains why many components of RNP granules, and other large dynamic assemblies, contain IDRs linked to specific protein-protein or protein-RNA interaction modules. We suggest assemblies based on combinations of specific interactions and promiscuous IDRs are common features of eukaryotic cells.</pubmed_abstract><journal>Cell reports</journal><pubmed_title>Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly.</pubmed_title><pmcid>PMC5824733</pmcid><funding_grant_id>GM063235</funding_grant_id><funding_grant_id>R01 GM045443</funding_grant_id><funding_grant_id>T32 GM065103</funding_grant_id><funding_grant_id>T32 GM142607</funding_grant_id><funding_grant_id>HCIA grant</funding_grant_id><funding_grant_id>GM045443</funding_grant_id><funding_grant_id>R01-GM56322</funding_grant_id><funding_grant_id>I-1544</funding_grant_id><funding_grant_id>T32 GM008759</funding_grant_id><pubmed_authors>Protter DSW</pubmed_authors><pubmed_authors>Rao BS</pubmed_authors><pubmed_authors>Van Treeck B</pubmed_authors><pubmed_authors>Mizoue L</pubmed_authors><pubmed_authors>Lin Y</pubmed_authors><pubmed_authors>Rosen MK</pubmed_authors><pubmed_authors>Parker R</pubmed_authors><view_count>60</view_count></additional><is_claimable>false</is_claimable><name>Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly.</name><description>Eukaryotic cells contain large RNA-protein assemblies referred to as RNP granules, whose assembly is promoted by both traditional protein interactions and intrinsically disordered protein domains. Using RNP granules as an example, we provide evidence for an assembly mechanism of large cellular structures wherein specific protein-protein or protein-RNA interactions act together with promiscuous interactions of intrinsically disordered regions (IDRs). This synergistic assembly mechanism illuminates RNP granule assembly and explains why many components of RNP granules, and other large dynamic assemblies, contain IDRs linked to specific protein-protein or protein-RNA interaction modules. We suggest assemblies based on combinations of specific interactions and promiscuous IDRs are common features of eukaryotic cells.</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Feb</publication><modification>2024-12-04T06:02:34.098Z</modification><creation>2019-03-26T23:03:53Z</creation></dates><accession>S-EPMC5824733</accession><cross_references><pubmed>29425497</pubmed><doi>10.1016/j.celrep.2018.01.036</doi></cross_references></HashMap>