Nucleoporins (Nups) represent a range of proteins most known for composing the macromolecular assembly of the nuclear pore complex (NPC). Among them, the family of intrinsically disordered proteins (IDPs) phenylalanine-glycine (FG) rich Nups, form the permeability barrier and coordinate the high-speed nucleocytoplasmic transport in a selective way. Those FG-Nups have been demonstrated to participate in various biological processes besides nucleocytoplasmic transport. The high number of accessible hydrophobic motifs of FG-Nups potentially gives rise to this multifunctionality, enabling them to form unique microenvironments. In this review, we discuss the multifunctionality of disordered and F-rich Nups and the diversity of their localizations, emphasizing the important roles of those Nups in various regulatory and metabolic processes.
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Cover Image
Cover Image
The plasma membrane of lymphocytes is highly compartmentalized in so-called nanodomains or protein islands. Proteins such as Caveolin-1 (pink), tetraspanins (blue) or flotillins (violet) define these protein islands and thereby regulate the functioning of the immune system. In this issue (see pages 2387–2397), Schaffer and Minguet discuss the importance of these protein islands regarding lymphocyte activation and the development of immunopathologies. This cover artwork has been created by Susana Minguet.
Multifunctionality of F-rich nucleoporins
Nike Heinß, Mikhail Sushkin, Miao Yu, Edward A. Lemke; Multifunctionality of F-rich nucleoporins. Biochem Soc Trans 18 December 2020; 48 (6): 2603–2614. doi: https://doi.org/10.1042/BST20200357
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