Article
 

Polybivalency and Disordered Proteins in Ordering Macromolecular Assemblies

Público Deposited

Contenido Descargable

Descargar PDF
https://ir.library.oregonstate.edu/concern/articles/8s45qb90t

Descriptions

Attribute NameValues
Creator
Abstract
  • 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, are core components, respectively, of cytoplasmic dynein, bicoid mRNA localization apparatus, and nuclear pore complexes. In all three systems, the hub protein LC8 recognizes on the IDP, short linear motifs that are fully disordered in the apo form, but adopt a β-strand when bound to LC8. The IDP/LC8 complex forms a bivalent scaffold primed to bind additional bivalent ligands. Scaffold formation also promotes self-association and/or higher order organization of the IDP components at a site distant from LC8 binding. Rigorous thermodynamic analyses imply that association of additional bivalent ligands is driven by entropic effects where the first binding event is weak but subsequent binding of additional ligands occurs with higher affinity. Here, we review specific examples of macromolecular assemblies in which polybivalency of aligned IDP duplexes not only enhances binding affinity and results in formation of a stable complex but also compensates unfavorable steric and enthalpic interactions. We propose that polybivalent scaffold assembly involving IDPs and LC8-like proteins is a general process in the cell biology of a class of multi-protein structures that are stable yet fine-tuned for diverse cellular requirements.
  • Keywords: Poly-bivalent scaffold, Macromolecular assembly, LC8, Bivalency, Intrinsically disordered proteins, Enthalpy–entropy compensation
Resource Type
DOI
Fecha Disponible
Fecha de Emisión
Citation
  • Barbar, E., & Nyarko, A. (2015). Polybivalency and disordered proteins in ordering macromolecular assemblies. Seminars in Cell & Developmental Biology, 37, 20-25. doi:10.1016/j.semcdb.2014.09.016
Journal Title
Journal Volume
  • 37
Declaración de derechos
Funding Statement (additional comments about funding)
  • This work was supported, in whole or in part, by National Institutes of Health Grant GM 084276.
Publisher
Peer Reviewed
Language
Replaces

Relaciones

Parents:

This work has no parents.

Elementos

Miniatura Título Fecha de subida Visibilidad Acciones
file details BarbarElisarBiochemistryBiophysicsPolybivalencyDisorderedProteins.pdf 07/26/2017 Público
file details BarbarElisarBiochemistryBiophysicsPolybivalencyDisorderedProteins(GraphicalAbstract).pdf 07/26/2017 Público