Eukaryotic ribosome biogenesis involves ~200 assembly
factors, but how these contribute to ribosome
maturation is poorly understood. Here, we
identify a network of factors on the nascent 60S subunit
that actively remodels preribosome structure. At its hub is
Rsa4, a direct substrate of the force-generating ATPase
Rea1. We show that...
Eukaryotic ribosome biogenesis involves ~200 assembly
factors, but how these contribute to ribosome
maturation is poorly understood. Here, we
identify a network of factors on the nascent 60S subunit
that actively remodels preribosome structure. At its hub is
Rsa4, a direct substrate of the force-generating ATPase
Rea1. We show that...
Intrinsically disordered proteins (IDPs) are prevalent in macromolecular assemblies and are
thought to mediate protein recognition in complex regulatory processes and signaling pathways. The
formation of a polybivalent scaffold is a key process by which IDPs drive early steps in macromolecular
assemblies. Three intrinsically disordered proteins, IC, Swallow and Nup159,...
Intrinsically disordered proteins (IDPs) are prevalent in macromolecular assemblies and are
thought to mediate protein recognition in complex regulatory processes and signaling pathways. The
formation of a polybivalent scaffold is a key process by which IDPs drive early steps in macromolecular
assemblies. Three intrinsically disordered proteins, IC, Swallow and Nup159,...
Dynein light chain LC8 is a small, dimeric, and very highly conserved globular protein that is an integral part of the dynein and myosin molecular motors but appears to have a broader role in multiple protein complexes unrelated to molecular motors. LC8 binds to two families of targets: those having...
Dynein light chain LC8 is a small, dimeric, and very highly conserved globular protein that is an integral part of the dynein and myosin molecular motors but appears to have a broader role in multiple protein complexes unrelated to molecular motors. LC8 binds to two families of targets: those having...
Intrinsically disordered protein (IDP) duplexes composed of two IDP chains cross-linked by bivalent partner proteins form scaffolds for assembly of multiprotein complexes. The N-terminal domain of dynein intermediate chain (N-IC) is one such IDP that forms a bivalent scaffold with multiple dynein light chains including LC8, a hub protein that...
Intrinsically disordered proteins (IDPs) are prevalent in macromolecular assemblies and are thought to mediate protein recognition in complex regulatory processes and signaling pathways. The formation of a polybivalent scaffold is a key process by which IDPs drive early steps in macromolecular assemblies. Three intrinsically disordered proteins, IC, Swallow and Nup159,...
Nuclear pore complexes (NPCs) are huge assemblies formed from ~30 different nucleoporins, typically organized in subcomplexes. One module, the conserved Nup82 complex at the cytoplasmic face of NPCs, is crucial to terminate mRNA export. To gain insight into the structure, assembly, and function of the cytoplasmic pore filaments, we reconstituted...
The following corrections appear in the attached pdf labelled "Correction to Version of Record". The authors inadvertently omitted Woonghee Lee from the list of authors. The corrected author list and affiliations are noted. Revised acknowledgment paragraphs including Woonghee Lee’s funding source and contribution also appear in the correction.
In addition,...
