RanGTP Targets p97 to RanBP2, a Filamentous Protein Localized at the Cytoplasmic Periphery of the Nuclear Pore Complex

Delphin, Christian; Guan, Tinglu; Melchior, Frauke; Gerace, Larry

doi:10.1091/mbc.8.12.2379

Cited by 135 publications

(138 citation statements)

References 61 publications

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“…Although a classification of the antigens detected using the sera of 18 astrocytoma patients is difficult, it is intriguing that many of them are involved in gene expression and proliferation: the son gene encodes a conserved DNA binding protein mapping to human chromosome 21; 10 the human nucleoside diphosphate kinase B, which is encoded by the gene nm23-H2, has the distinctive property of stimulating gene transcription; 11 Ranbinding protein 2, a protein containing FG repeat motifs and 4 binding sites for the guanosine triphosphatase Ran, which is localized at the cytoplasmic periphery of the nuclear pore complex, is believed to play a critical role in nuclear protein import 12 and in the nuclear export pathway; 13 and finally, BI-1, which is a regulator of cell death pathways controlled by Bcl-2 and BAX. 14 When overexpressed in mammalian cells, BI-1 suppresses apoptosis induced by Bax, etoposide, staurosporine and growth factor deprivation, but not by Fas (CD95).…”

Section: Discussionmentioning

confidence: 99%

Analysis of the antibody repertoire of astrocytoma patients against antigens expressed by gliomas

Schmits

Cochlovius

Treitz

et al. 2001

Intl Journal of Cancer

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The molecular characterization of antigens preferentially or exclusively expressed by astrocytomas and recognized by the autologous immune system are a prerequisite for the development of specific vaccines. To identify such antigens, we screened 5 cDNA expression libraries derived from astrocytomas and other gliomas for reactivity with high-titered IgG antibodies in the sera of astrocytoma patients using SEREX, the serologic identification of antigens by recombinant cDNA expression cloning. Autologous and allogeneic SEREX analysis of >5 ؋ 10 6 clones with the sera of 18 astrocytoma patients revealed 10 antigens: the differentiation antigen glial fibrillary acidic protein (GFAP), Bax-inhibitor 1 (which was overexpressed in all glioma samples tested), 3 other molecules involved in the regulation of gene expression and proliferation (the nm23-H2-encoded nucleoside diphosphate kinase B, the Ran binding protein-2 and a DNA binding protein encoded by the son gene), SP40,40 (a complement inhibitory molecule), the chaperonin TCP-1, calnexin and 2 new gene products. No immune responses were detected against the "shared tumor" or "cancer testis antigens" that are regularly expressed in gliomas. Antibody responses in astrocytoma patients against antigens expressed by gliomas were rare and, with the exception of Bax-inhibitor 1 and the product of the son gene, were also found in apparently healthy controls. We conclude that although astrocytomas express a broad spectrum of antigens, they elicit antibody responses only rarely, most likely because of their intrinsic immunosuppressive effects.

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Section: Discussionmentioning

confidence: 99%

Analysis of the antibody repertoire of astrocytoma patients against antigens expressed by gliomas

Schmits

Cochlovius

Treitz

et al. 2001

Intl Journal of Cancer

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“…Firstly, they are not detected in 3D reconstructions (Yang et al, 1998). Secondly, it has been shown that the Ran binding nucleoporin, Nup358, is a major constituent of the filaments (Wu et al, 1995;Delphin et al, 1997;Walther and Pickersgill et al, 2002), possibly even the filament itself, and there is apparently no similar protein in yeast. Despite the fact that Nup358 appears to be the major component of cytoplasmic filaments in the vertebrate NPC (Walther and Pickersgill et al, 2002) in yeast a similar filament structure could be constructed from one or more different proteins.…”

Section: Cytoplasmic Filamentsmentioning

confidence: 99%

“…The ring consists of at least three sequential components: (1) the star ring which lies on and is embedded in the membrane; (2) the thin ring which lies on top of the star ring and then (3) eight bipartite subunits that are molded onto the thin ring (Goldberg and Allen, 1992).The star ring has only been detected by field emission scanning electron microscopy (feSEM) (Goldberg and Allen, 1996) and may form part of the cytoplasmic ring and transmembrane vertical domains seen in 3D reconstructions (Akey and Radermacher, 1993), as the tips of its triangular shaped subunits appear to be embedded in the membrane. Filaments extend from the cytoplasmic ring into the cytoplasm and contain the Ran binding protein Nup358 (Wu et al, 1995;Delphin et al, 1997;Walther and Pickersgill et al, 2002). They appear to have controlled dynamics , but are not essential in at least some nuclear transport pathways (Walther and Pickersgill et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments

Киселева

Allen

Rutherford

et al. 2004

Journal of Structural Biology

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The full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-pro t purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. AbstractThe nuclear pore complex (NPC) controls transport of macromolecules across the nuclear envelope. It is large and complex but appears to consist of only ~30 different proteins despite its mass of >60 MDa. Vertebrate NPC structure has been analyzed by several methods giving a comprehensive architectural model. Despite our knowledge of yeast nucleoporins, structural data is more limited and suggests the basic organization is similar to vertebrates, but may lack some peripheral and other components. Using field emission scanning electron microscopy to probe NPC structure we found that the yeast, like higher eukaryotic, NPCs contain similar peripheral components. We can detect cytoplasmic rings and evidence of nucleoplasmic rings in yeasts. A filamentous basket is present on the nucleoplasmic face and evidence for cytoplasmic filaments is shown. We observe a central structure, possibly the transporter, that which may be linked to the cytoplasmic ring by internal filaments. Immuno-gold labeling suggests that Nup159p may be attached to the cytoplasmic ring, whereas Nup116p may be associated, partly, with the cytoplasmic filaments. Analysis of a Nup57p mutant suggested a role in maintaining the stability of cytoplasmic components of the NPC. We conclude that peripheral NPC components appear similar in yeasts compared to higher organisms and present a revised model for yeast NPC structural composition.4

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“…The filaments are composed primarily of Nup358 (12,47,50), with Nup214 and Nup88 existing as a complex on the cytoplasmic face of the NPC (3,28,39). By projecting into the cytoplasm, the filaments are in a position to interact with HSV-1 capsids.…”

mentioning

confidence: 99%

Herpes Simplex Virus Replication: Roles of Viral Proteins and Nucleoporins in Capsid-Nucleus Attachment

Copeland

Newcomb

Brown

2009

J Virol

140

137

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Replication of herpes simplex virus type 1 (HSV-1) involves a step in which a parental capsid docks onto a host nuclear pore complex (NPC). The viral genome then translocates through the nuclear pore into the nucleoplasm, where it is transcribed and replicated to propagate infection. We investigated the roles of viral and cellular proteins in the process of capsid-nucleus attachment. Vero cells were preloaded with antibodies specific for proteins of interest and infected with HSV-1 containing a green fluorescent protein-labeled capsid, and capsids bound to the nuclear surface were quantified by fluorescence microscopy. Results showed that nuclear capsid attachment was attenuated by antibodies specific for the viral tegument protein VP1/2 (UL36 gene) but not by similar antibodies specific for UL37 (a tegument protein), the major capsid protein (VP5), or VP23 (a minor capsid protein). Similar studies with antibodies specific for nucleoporins demonstrated attenuation by antibodies specific for Nup358 but not Nup214. The role of nucleoporins was further investigated with the use of small interfering RNA (siRNA). Capsid attachment to the nucleus was attenuated in cells treated with siRNA specific for either Nup214 or Nup358 but not TPR. The results are interpreted to suggest that VP1/2 is involved in specific attachment to the NPC and/or in migration of capsids to the nuclear surface. Capsids are suggested to attach to the NPC by way of the complex of Nup358 and Nup214, with high-resolution immunofluorescence studies favoring binding to Nup358.

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RanGTP Targets p97 to RanBP2, a Filamentous Protein Localized at the Cytoplasmic Periphery of the Nuclear Pore Complex

Cited by 135 publications

References 61 publications

Analysis of the antibody repertoire of astrocytoma patients against antigens expressed by gliomas

Analysis of the antibody repertoire of astrocytoma patients against antigens expressed by gliomas

Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments

Herpes Simplex Virus Replication: Roles of Viral Proteins and Nucleoporins in Capsid-Nucleus Attachment

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