Fifty Years of Nuclear Pores and Nucleocytoplasmic Transport Studies

Floch, Aurélie G; Palancade, Benoı̂t; Doye, Valérie

doi:10.1016/b978-0-12-417160-2.00001-1

Cited by 57 publications

(46 citation statements)

References 166 publications

(149 reference statements)

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“…Tethered by this membrane-embedded central framework, peripheral NPC components (notably a subset of Nups containing Phe-Gly repeats, FG-Nups) extend into the central pore channel and into the cytoplasm and the nucleoplasm, where they form cytoplasmic filaments and the nuclear pore basket respectively (reviewed in refs. [13][14][15][16] (Fig. 1A).…”

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confidence: 99%

Probing nuclear pore complex architecture with proximity-dependent biotinylation

Kim

Zhu

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Proximity-dependent biotin identification (BioID) is a method for identifying protein associations that occur in vivo. By fusing a promiscuous biotin ligase to a protein of interest expressed in living cells, BioID permits the labeling of proximate proteins during a defined labeling period. In this study we used BioID to study the human nuclear pore complex (NPC), one of the largest macromolecular assemblies in eukaryotes. Anchored within the nuclear envelope, NPCs mediate the nucleocytoplasmic trafficking of numerous cellular components. We applied BioID to constituents of the Nup107-160 complex and the Nup93 complex, two conserved NPC subcomplexes. A strikingly different set of NPC constituents was detected depending on the position of these BioID-fusion proteins within the NPC. By applying BioID to several constituents located throughout the extremely stable Nup107-160 subcomplex, we refined our understanding of this highly conserved subcomplex, in part by demonstrating a direct interaction of Nup43 with Nup85. Furthermore, by using the extremely stable Nup107-160 structure as a molecular ruler, we defined the practical labeling radius of BioID. These studies further our understanding of human NPC organization and demonstrate that BioID is a valuable tool for exploring the constituency and organization of large protein assemblies in living cells.

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confidence: 99%

Probing nuclear pore complex architecture with proximity-dependent biotinylation

Kim

Zhu

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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472

459

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“…First, the NPCs remain the essential and very efficient selective gate in transporting thousands of various molecules per NPC per second, [2][3][4] while large ribonucleoprotein complexes can also exit the nucleus via nuclear membrane budding. 10 Second, recent evidence suggests that the NPCs are not only essential for nuclear transport, but also play roles in tissue-specific and developmental functions.…”

Section: An Overview Of the Npcs And Fg-nupsmentioning

confidence: 99%

“…10 The size of the NPC is estimated to be »60 MD in yeast and »120 MD in vertebrates. 2,4 This super-structure complex is comprised of 3 functional groups of Nups: transmembrane Nups (Poms) that anchor to the NPC in the nuclear envelope, structural Nups that make up the NPC scaffold, and the intrinsically disordered Nups that constitute the permeability barrier with their disordered regions ( Table 1). Each of these Nups is present in 1, 2, or 4 copies on each of the 8 spokes [8-fold rotational symmetry, although 9-fold rotational symmetry is occasionally observed 11 ].…”

Section: An Overview Of the Npcs And Fg-nupsmentioning

confidence: 99%

“…Molecules essential for protein synthesis (such as tRNAs, mRNAs, and pre-ribosomal subunits produced in the nucleus) are exported to the cytoplasm, while nuclear proteins synthesized in the cytoplasm (such as histones and transcription factors) are imported into the nucleus. [1][2][3][4] This bidirectional transport is mediated almost exclusively via the nuclear pore complex (NPC), 3,5 a unique machinery that consists of approximately 30 different types of nucleoporins (Nups). In eukaryotic cells, approximately one third of these Nups are intrinsically disordered proteins, with multiple phenylalanine-glycine (FG) repeats that have characteristic unstructured nature.…”

Section: Introductionmentioning

confidence: 99%

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The selective permeability barrier in the nuclear pore complex

Goryaynov

Yang

2016

Nucleus

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The nuclear pore complex (NPC) mediates the shuttle transport of macromolecules between the nucleus and cytoplasm in eukaryotic cells. The permeability barrier formed by intrinsically disordered phenylalanine-glycine-rich nucleoporins (FG-Nups) in the NPC functions as the critical selective control for nucleocytoplasmic transport. Signal-independent small molecules (< 40 kDa) passively diffuse through the pore, but passage of large cargo molecules is inhibited unless they are chaperoned by nuclear transport receptors (NTRs). NTRs are capable of interacting with FG-Nups and guide the cargos to cross the barrier by facilitated diffusion. The native conformation of the FGNups permeability barrier and the competition among multiple NTRs interacting with this barrier in the native NPCs are the 2 core questions still being highly debated in the field. Recently, we applied high-speed super-resolution fluorescence microscopy to map out the natural structure of the FGNups barrier and determined the competition among multiple NTRs as they interact with the barrier in the native NPCs. In this extra-view article, we will review the current understanding in the configuration and function of FG-Nups barrier and highlight the new evidence obtained recently to answer the core questions in nucleocytoplasmic transport.

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“…Most exchanges between these two compartments take place through nuclear pore complexes (NPCs), which are megadalton-size protein assemblies composed of ,30 distinct proteins (nucleoporins, Nups), each present in multiple copies per NPC (reviewed in Aitchison and Rout, 2012;Floch et al, 2014). Although small molecules can freely pass through the NPCs, large macromolecules undergo highly selective nuclear import and/or export processes.…”

Section: Introductionmentioning

confidence: 99%

Nuclear pore targeting of the yeast Pom33 nucleoporin depends on karyopherin- and lipid-binding

Floch

Tareste

Fuchs

et al. 2014

Journal of Cell Science

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Pom33 is an integral membrane protein of the yeast nuclear pore complex (NPC), required for proper NPC distribution and assembly. To characterize Pom33 NPC-targeting determinants, we performed immunoprecipitation experiments followed by mass spectrometry analyses. This identified a novel Pom33 partner, the nuclear import factor Kap123. In vitro experiments revealed a direct interaction between Pom33 C-terminal domain (CTD) and Kap123. In silico analysis predicted the presence of two amphipathic α-helices within Pom33-CTD. Circular dichroism and liposome co-flotation assays showed that this domain is able to fold into α-helices in the presence of liposomes and preferentially binds to highly curved lipid membranes. When expressed in yeast, under conditions abolishing Pom33-CTD membrane association, this domain behaves as a Kap123-dependent nuclear localization signal (NLS). While deletion of Pom33 C-terminal domain (Pom33ΔCTD-GFP) impairs Pom33 stability and NPC targeting, mutants affecting either Kap123 binding or the amphipathic properties of the α-helices do not display any detectable defect. However, combined impairment of lipid and Kap123 binding affects Pom33 targeting to NPCs. These data highlight the requirement of multiple determinants and mechanisms for proper NPC localization of Pom33.

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Fifty Years of Nuclear Pores and Nucleocytoplasmic Transport Studies

Cited by 57 publications

References 166 publications

Probing nuclear pore complex architecture with proximity-dependent biotinylation

Probing nuclear pore complex architecture with proximity-dependent biotinylation

The selective permeability barrier in the nuclear pore complex

Nuclear pore targeting of the yeast Pom33 nucleoporin depends on karyopherin- and lipid-binding

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