TY - JOUR T1 - Intrinsically disordered regions contribute promiscuous interactions to RNP granule assembly JF - bioRxiv DO - 10.1101/147561 SP - 147561 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 Y1 - 2017/01/01 UR - http://biorxiv.org/content/early/2017/06/12/147561.abstract N2 - 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. ER -