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Cell Rep. 2018 Feb 6;22(6):1401-1412. doi: 10.1016/j.celrep.2018.01.036.

Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly.

Author information

1
Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado, Boulder, CO 80309, USA.
2
Department of Biophysics, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
3
Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado, Boulder, CO 80309, USA. Electronic address: roy.parker@colorado.edu.

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.

KEYWORDS:

Dhh1; P-body; RNP granule; intrinsically disordered; phase separation

PMID:
29425497
PMCID:
PMC5824733
DOI:
10.1016/j.celrep.2018.01.036
[Indexed for MEDLINE]
Free PMC Article

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