title: The Multiple Faces of Disordered Nucleoporins.
abstract: An evolutionary advantage of intrinsically disordered proteins (IDPs) is their ability to bind a variety of folded proteins-a paradigm that is central to the nucleocytoplasmic transport mechanism, in which nuclear transport receptors mediate the translocation of various cargo through the nuclear pore complex by binding disordered phenylalanine-glycine-rich nucleoporins (FG-Nups). FG-Nups are highly dynamic, which poses a substantial problem when trying to determine precisely their function using common experimental approaches. FG-Nups have been studied under a variety of conditions, ranging from those that constitute single-molecule measurements to physiological concentrations at which they can form supramolecular structures. In this review, I describe the physicochemical properties of FG-Nups and compare them to those of other disordered systems, including well-studied IDPs. From this comparison, it is apparent that FG-Nups not only share some properties with IDPs in general but also possess unique characteristics that might be key to their central role in the nucleocytoplasmic transport machinery.
authors.affiliation: Structural and Computational Biology Unit, Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany. Electronic address: lemke@embl.de.
authors.forename: Edward A
authors.initials: EA
authors.lastname: Lemke
mesh_terms: D021581:Active Transport, Cell Nucleus / Q000502:physiology; D003593:Cytoplasm / Q000378:metabolism / Q000502:physiology; D005998:Glycine / Q000378:metabolism; D006801:Humans; D022022:Nuclear Pore / Q000378:metabolism* / Q000502:physiology*; D028861:Nuclear Pore Complex Proteins / Q000378:metabolism*; D010649:Phenylalanine / Q000378:metabolism; D017510:Protein Folding
chemical_list: D028861:Nuclear Pore Complex Proteins; D010649:Phenylalanine; D005998:Glycine
keywords: intrinsically disordered proteins; nucleocytoplasmic transport; phase separation; protein folding and dynamics; protein moonlighting