title: Transport Selectivity of Nuclear Pores, Phase Separation, and Membraneless Organelles.
abstract: Nuclear pore complexes (NPCs) provide a selective passageway for receptor-mediated active transport between nucleus and cytoplasm, while maintaining the distinct molecular compositions of both compartments at large. In this review we discuss how NPCs gain a remarkable sorting selectivity from non-globular FG domains and their phase separation into dense polymer meshworks. The resulting sieve-like FG hydrogels are effective barriers to normal macromolecules but are at the same time highly permeable to shuttling nuclear transport receptors, which bind to FG motifs as well as to their designated cargoes. Phase separation driven by disordered protein domains was recently also recognized as being pivotal to the formation of membraneless organelles, making it an important emerging principle in cell biology.
authors.affiliation: Department of Biochemistry, Stanford University, Stanford, CA, USA.
authors.forename: H Broder
authors.initials: HB
authors.lastname: Schmidt
authors.affiliation: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. Electronic address: goerlich@mpibpc.mpg.de.
authors.forename: Dirk
authors.initials: D
authors.lastname: Görlich
mesh_terms: D021581:Active Transport, Cell Nucleus; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D006801:Humans; D022022:Nuclear Pore / Q000378:metabolism*; D015388:Organelles / Q000378:metabolism*
keywords: FG domains; intracellular phase separation; intrinsically disordered proteins; nuclear pore; protein disorder; protein phases