Nup180, a novel nuclear pore complex protein localizing to the cytoplasmic ring and associated fibrils.

Wilken, Norbert; Kossner, Ursula; Senécal, Jean‐Luc; Scheer, Ulrich; Dabauvalle, Marie-Christine

doi:10.1083/jcb.123.6.1345

Cited by 46 publications

(27 citation statements)

References 67 publications

(89 reference statements)

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“…The mass of the 55-kD plant GlcNAc protein (60 kD after 3H-galactose incorporation) raises the possibility that it may be the plant homolog of vertebrate p62. p62 is found in multiple copies on the cytoplasmic and/or the nucleoplasmic faces of the central NPC regions (Davis and Blobel, 1986;Dabauvalle et al, 1990;Cordes et al, 1991;Wilken et al, 1993). However, a monoclonal antibody against rat p62 (mAb414; Davis and Blobel, 1986) did not detect plant NPC proteins of similar mass (A. Heese-Peck and N.V. Raikhel, unpublished results).…”

Section: Proteins Modified By Glcnac Are Located At the Npcmentioning

confidence: 99%

Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine.

et al. 1995

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Only a few nuclear pore complex (NPC) proteins, mainly in vertebrates and yeast but none in plants, have been well characterized. As an initial step to identify plant NPC proteins, we examined whether NPC proteins from tobacco are modified by N-acetylglucosamine (GlcNAc). Using wheat germ agglutinin, a lectin that binds specifically to GlcNAc in plants, specific labeling was often found associated with or adjacent to NPCs. Nuclear proteins containing GlcNAc can be partially extracted by 0.5 M salt, as shown by a wheat germ agglutinin blot assay, and at least eight extracted proteins were modified by terminal GlcNAc, as determined by in vitro galactosyltransferase assays. Sugar analysis indicated that the plant glycans with terminal GlcNAc differ from the single O-linked GlcNAc of vertebrate NPC proteins in that they consist of oligosaccharides that are larger in size than five GlcNAc residues. Most of these appear to be bound to proteins via a hydroxyl group. This novel oligosaccharide modification may convey properties to the plant NPC that are different from those of vertebrate NPCs.

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Section: Proteins Modified By Glcnac Are Located At the Npcmentioning

confidence: 99%

Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine.

et al. 1995

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“…Some authors have suggested that these cytoplasmic dots represent either AL (Greber et al 1990; Wozniak and Blobel 1992;Wilken et al 1993) or aggregates of nucleoporins (Carmo-Fonseca et al 1991). However, in these studies the cytoplasmic structures were not further characterized by electron microscopy, and thus the significance of this staining remained unknown.…”

Section: Introductionmentioning

confidence: 98%

Cytoplasmic annulate lamellae in cultured cells: composition, distribution, and mitotic behavior

Cordes

Reidenbach

Franke

1996

Cell and Tissue Research

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We have used antibodies against different proteins of the nuclear pore complex to identify cytoplasmic annulate lamellae by immunocytochemistry at the light- and electron-microscopic level in various lines of cultured mammalian cells. Although annulate lamellae (AL) are seldom observed in some cell lines, they occur in large numbers in other lineages, also with cell-type-specific size distributions. AL are especially abundant and prominent in African green monkey kidney epithelial cells of line RC37 and bovine mammary gland epithelial, cells of line BMGE. We have studied the distribution of AL in relation to other organelles by using double-label immunofluorescence microscopy and have demonstrated a significant relationship between AL and rough endoplasmic reticulum. We have further shown that AL are disassembled during prophase and reassembled at the end of mitosis, almost concomitantly with the disassembly and reassembly of the nuclear envelope. Cultured mammalian cells that are rich in AL can therefore be used as suitable models for studies of the biogenesis of these lamellae, which can conveniently be detected by immunofluorescence microscopy.

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“…This substance, which binds to O-linked N-acetylglucosamine moieties present on certain nucleoporins (45)(46)(47), effectively blocks receptor-mediated translocation (48 -52) but has little effect on the diffusion of intermediate-sized polymers and proteins (49,50,53). Electron microscopy studies indicate that wheat germ agglutinin accumulates mostly, although not exclusively, in the central region of the pores (52,54,55) and does not prevent binding of NLS-carrying cargoes to the surface of the pores (48, 52,56). The different effects exerted by wheat germ agglutinin on passive and facilitated transport through NPCs are naturally explained by the existence of separate routes of transport for each mode.…”

Section: Segregation Of Transport Modes In Nuclear Poresmentioning

confidence: 99%

Passive and Facilitated Transport in Nuclear Pore Complexes Is Largely Uncoupled

Naim

Brumfeld

Kapon

et al. 2007

Journal of Biological Chemistry

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Nuclear pore complexes provide the sole gateway for the exchange of material between nucleus and cytoplasm of interphase eukaryotic cells. They support two modes of transport: passive diffusion of ions, metabolites, and intermediate-sized macromolecules and facilitated, receptor-mediated translocation of proteins, RNA, and ribonucleoprotein complexes. It is generally assumed that both modes of transport occur through a single diffusion channel located within the central pore of the nuclear pore complex. To test this hypothesis, we studied the mutual effects between transporting molecules utilizing either the same or different modes of translocation. We find that the two modes of transport do not interfere with each other, but molecules utilizing a particular mode of transport do hinder motion of others utilizing the same pathway. We therefore conclude that the two modes of transport are largely segregated.Eukaryotic cell nuclei are separated from the cytoplasm by a double lipid bilayer system known as the nuclear envelope (NE).2 Exchange of material between the two compartments proceeds through nuclear pore complexes (NPCs), large protein assemblies that span the NE and provide the sole medium for exchange. The vertebrate NPC has a molecular mass of ϳ125 MDa (1) and is made up of ϳ30 different proteins, called nucleoporins, most of which are present in multiples of eight (2, 3). The core of the NPC consists of a symmetrical framework, measuring ϳ120 ϫ 90 nm, which is made of two coaxial rings sandwiching a wheel-like array of eight spoke-shaped domains. The spoke-ring assembly encircles the central pore channel, which resembles an hourglass 45-50 nm wide at its waist (4 -7). In addition to the central framework, NPCs contain peripheral structures, which are anchored to the ring moieties of the spoke-ring assembly and serve as docking sites for nuclear transport receptors and effectors. These structures include eight short (ϳ50 nm) filaments that protrude toward the cytoplasm and a massive, fish trap-like structure, termed the nuclear basket, which extends into the nucleus (4 -11). Yeast NPCs have an overall similar architecture but are smaller (3,(12)(13)(14).Transport across the NPC has been reviewed in detail (15-22) and can be divided into two modes. Small molecules, such as ions, metabolites, and intermediate-sized macromolecules, can pass unassisted by diffusion which becomes increasingly restricted as the particle approaches a size limit of ϳ10 nm in diameter (23,24). In contrast, proteins, RNAs, and their complexes are ushered selectively by dedicated soluble transport receptors, which recognize specific import (NLS) or nuclear export signal (NES) peptides displayed by the cargo. In most cases, assembly and disassembly of transport complexes in the appropriate cellular compartment are coordinated by the small GTPase Ran, which performs these activities by binding to transport receptors in its GTP-bound form. Facilitated translocation is often coupled to an input of metabolic energy that permits transport ...

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Nup180, a novel nuclear pore complex protein localizing to the cytoplasmic ring and associated fibrils.

Cited by 46 publications

References 67 publications

Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine.

Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine.

Cytoplasmic annulate lamellae in cultured cells: composition, distribution, and mitotic behavior

Passive and Facilitated Transport in Nuclear Pore Complexes Is Largely Uncoupled

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