Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics

• Published in: Nucleus (Austin, Tex.) Vol. 15; no. 1; p. 2399247
• Main Authors: Matsuda, Atsushi, Mansour, Abdullah, Mofrad, Mohammad R K
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 01.12.2024; Taylor & Francis Group
• Subjects: Animals; FG-Nups; Glycine - chemistry; Glycine - metabolism; Humans; intrinsically disordered proteins; Intrinsically Disordered Proteins - chemistry; Intrinsically Disordered Proteins - metabolism; Nuclear Pore - chemistry; Nuclear Pore - metabolism; nuclear pore complex; Nuclear Pore Complex Proteins - chemistry; Nuclear Pore Complex Proteins - metabolism; Phenylalanine - chemistry; Phenylalanine - metabolism; polymer physics; Polymers - chemistry; Polymers - metabolism; Review; selective permeability; nuclear pore complex; selective permeability; polymer physics; FG-Nups; intrinsically disordered proteins
• ISSN: 1949-1042; 1949-1034; 1949-1042
• DOI: 10.1080/19491034.2024.2399247

The nuclear pore complex (NPC) is a critical gateway regulating molecular transport between the nucleus and cytoplasm. It allows small molecules to pass freely, while larger molecules require nuclear transport receptors to traverse the barrier. This selective permeability is maintained by phenylalanine-glycine-rich nucleoporins (FG-Nups), intrinsically disordered proteins that fill the NPC's central channel. The disordered and flexible nature of FG-Nups complicates their spatial characterization with conventional structural biology techniques. To address this challenge, polymer physics offers a valuable framework for describing FG-Nup behavior, reducing their complex structures to a few key parameters. In this review, we explore how polymer physics models FG-Nups using these parameters and discuss experimental efforts to quantify them in various contexts, providing insights into the conformational properties of FG-Nups.