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Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly

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 struc...

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Detalles Bibliográficos
Autores principales: Protter, David S.W., Rao, Bhalchandra S., Van Treeck, Briana, Lin, Yuan, Mizoue, Laura, Rosen, Michael K., Parker, Roy
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5824733/
https://www.ncbi.nlm.nih.gov/pubmed/29425497
http://dx.doi.org/10.1016/j.celrep.2018.01.036
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author Protter, David S.W.
Rao, Bhalchandra S.
Van Treeck, Briana
Lin, Yuan
Mizoue, Laura
Rosen, Michael K.
Parker, Roy
author_facet Protter, David S.W.
Rao, Bhalchandra S.
Van Treeck, Briana
Lin, Yuan
Mizoue, Laura
Rosen, Michael K.
Parker, Roy
author_sort Protter, David S.W.
collection PubMed
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.
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spelling pubmed-58247332018-02-23 Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly Protter, David S.W. Rao, Bhalchandra S. Van Treeck, Briana Lin, Yuan Mizoue, Laura Rosen, Michael K. Parker, Roy Cell Rep Article 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. 2018-02-06 /pmc/articles/PMC5824733/ /pubmed/29425497 http://dx.doi.org/10.1016/j.celrep.2018.01.036 Text en This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article
Protter, David S.W.
Rao, Bhalchandra S.
Van Treeck, Briana
Lin, Yuan
Mizoue, Laura
Rosen, Michael K.
Parker, Roy
Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly
title Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly
title_full Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly
title_fullStr Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly
title_full_unstemmed Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly
title_short Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly
title_sort intrinsically disordered regions can contribute promiscuous interactions to rnp granule assembly
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5824733/
https://www.ncbi.nlm.nih.gov/pubmed/29425497
http://dx.doi.org/10.1016/j.celrep.2018.01.036
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