Journal
CELL REPORTS
Volume 22, Issue 6, Pages 1401-1412Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2018.01.036
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Funding
- HCIA grant from the Howard Hughes Medical Institute
- NIH [GM045443, R01-GM56322]
- Howard Hughes Medical Institute
- Welch Foundation [I-1544]
- [T32 GM063235]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM065103, T32GM008759, R01GM056322, R01GM045443] Funding Source: NIH RePORTER
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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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