Nuclear Pore Basket Proteins Are Tethered to the Nuclear Envelope and Can Regulate Membrane Curvature

• Published in: Developmental cell Vol. 33; no. 3; pp. 285 - 298
• Main Authors: Mészáros, Noémi, Cibulka, Jakub, Mendiburo, Maria Jose, Romanauska, Anete, Schneider, Maren, Köhler, Alwin
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 04.05.2015; Cell Press
• Subjects: Animals; Biological Transport - genetics; Biological Transport - physiology; Nuclear Envelope - metabolism; Nuclear Pore - metabolism; Nuclear Pore Complex Proteins - chemistry; Nuclear Pore Complex Proteins - genetics; Nuclear Pore Complex Proteins - metabolism; Protein Structure, Secondary; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism
• ISSN: 1534-5807; 1878-1551
• DOI: 10.1016/j.devcel.2015.02.017

Nuclear pore complexes (NPCs) are selective transport channels embedded in the nuclear envelope. The cylindrical NPC core forms a protein coat lining a highly curved membrane opening and has a basket-like structure appended to the nucleoplasmic side. How NPCs interact with lipids, promoting membrane bending and NPC integrity, is poorly understood. Here we show that the NPC basket proteins Nup1 and Nup60 directly induce membrane curvature by amphipathic helix insertion into the lipid bilayer. In a cell-free system, both Nup1 and Nup60 transform spherical liposomes into highly curved membrane structures. In vivo, high levels of the Nup1/Nup60 amphipathic helices cause deformation of the yeast nuclear membrane, whereas adjacent helical regions contribute to anchoring the basket to the NPC core. Basket amphipathic helices are functionally linked to distinct transmembrane nucleoporins of the NPC core, suggesting a key contribution to the membrane remodeling events that underlie NPC assembly. [Display omitted] •The nuclear pore basket is tethered to the nuclear envelope•Amphipathic helices within Nup1 and Nup60 bind and bend membranes•Basket-lipid interactions contribute to NPC integrity How nuclear pore complexes (NPCs) assemble and insert into the nuclear envelope is still unclear. Mészáros and Cibulka et al. find that nuclear pore basket proteins Nup1 and Nup60 can directly bind and remodel membranes via amphipathic helices, thereby promoting NPC and nuclear envelope integrity.