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Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.
Matsuda, Atsushi; Mansour, Abdullah; Mofrad, Mohammad R K.
Afiliación
  • Matsuda A; Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California Berkeley, Berkeley, CA, USA.
  • Mansour A; Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California Berkeley, Berkeley, CA, USA.
  • Mofrad MRK; Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California Berkeley, Berkeley, CA, USA.
Nucleus ; 15(1): 2399247, 2024 Dec.
Article en En | MEDLINE | ID: mdl-39282864
ABSTRACT
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Complejo Poro Nuclear / Proteínas Intrínsecamente Desordenadas Límite: Animals / Humans Idioma: En Revista: Nucleus Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Complejo Poro Nuclear / Proteínas Intrínsecamente Desordenadas Límite: Animals / Humans Idioma: En Revista: Nucleus Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos