PT  - JOURNAL ARTICLE
AU  - David S. W. Protter
AU  - Bhalchandra S. Rao
AU  - Briana Van Treeck
AU  - Yuan Lin
AU  - Laura Mizoue
AU  - Michael K. Rosen
AU  - Roy Parker
TI  - Intrinsically disordered regions contribute promiscuous interactions to RNP granule assembly
AID  - 10.1101/147561
DP  - 2017 Jan 01
TA  - bioRxiv
PG  - 147561
4099  - http://biorxiv.org/content/early/2017/06/12/147561.short
4100  - http://biorxiv.org/content/early/2017/06/12/147561.full
AB  - 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.