A Novel Complex of Nucleoporins, Which Includes Sec13p and a Sec13p Homolog, Is Essential for Normal Nuclear Pores

Siniossoglou, Symeoni; Wimmer, Christian; Rieger, Michael A.; Doye, Valérie; Tekotte, Hille; Weise, Christoph; Emig, Sonja; Segref, Alexandra; Hurt, Eduard C.

doi:10.1016/s0092-8674(00)80981-2

Cited by 308 publications

(400 citation statements)

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“…The consequences of Seh1 depletion on the delocalization of various nucleoporins from the NE was less pronounced compared with the effect of Nup133 or Nup107 siRNAs, suggesting a minor contribution of Seh1 to the overall function of the Nup107-160 complex in human cells. Yet, this phenotype was unexpected, because deletion of the Seh1 ortholog in S. cerevisiae, while affecting cell growth particularly at lower temperatures, does not induce any of the phenotypes observed for other constituents of the ScNup84 complex, namely, NPC clustering and growth defect at 37°C (Siniossoglou et al, 1996). While a decreased mAb414 labeling was recently reported in gp210-depleted cells (Cohen et al, 2003), such defects were not observed with siRNA duplexes targeting Tpr or Nup358/RanBP2 (Hase and Cordes, 2003;Salina et al, 2003).…”

Section: Seh1 Behaves As a Constituent Of The Nup107-160 Complexmentioning

confidence: 86%

“…In S. cerevisiae, this complex is formed by seven constituents: Nup84; Nup85; Nup120; the in vivo-cleaved carboxyterminal domain of Nup145 (Nup145-C); Seh1; a fraction of Sec13; and Nup133 (Siniossoglou et al, 1996;Teixeira et al, 1997;Allen et al, 2002;Lutzmann et al, 2002). Isolation under native conditions and in vitro reconstitution have further revealed the Y-shaped structure of this complex (Siniossoglou et al, 2000;Lutzmann et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…In addition, previous studies reported the cofractionation on sucrose gradients of Nup107, Nup96, and Sec13 together with a 37-kDa WD-repeat containing protein (Fontoura et al, 1999), subsequently identified as Nup37 (Cronshaw et al, 2002). Conversely, the S. cerevisiae Nup84 complex contains another WD-repeat nucleoporin, ScSeh1 (Siniossoglou et al, 1996), for which a potential higher eukaryote homologue has been identified (Cronshaw et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

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The Entire Nup107-160 Complex, Including Three New Members, Is Targeted as One Entity to Kinetochores in Mitosis

Loïodice

Alves

Rabut

et al. 2004

MBoC

254

240

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In eukaryotes, bidirectional transport of macromolecules between the cytoplasm and the nucleus occurs through elaborate supramolecular structures embedded in the nuclear envelope, the nuclear pore complexes (NPCs). NPCs are composed of multiple copies of ϳ30 different proteins termed nucleoporins, of which several can be biochemically isolated as subcomplexes. One such building block of the NPC, termed the Nup107-160 complex in vertebrates, was so far demonstrated to be composed of six different nucleoporins. Here, we identify three WD (Trp-Asp)-repeat nucleoporins as new members of this complex, two of which, Nup37 and Nup43, are specific to higher eukaryotes. The third new member Seh1 is more loosely associated with the Nup107-160 complex biochemically, but its depletion by RNA interference leads to phenotypes similar to knock down of other constituents of this complex. By combining green fluorescent protein-tagged nucleoporins and specific antibodies, we show that all the constituents of this complex, including Nup37, Nup43, Seh1, and Sec13, are targeted to kinetochores from prophase to anaphase of mitosis. Together, our results indicate that the entire Nup107-160 complex, which comprises nearly one-third of the so-far identified nucleoporins, specifically localizes to kinetochores in mitosis.

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Section: Seh1 Behaves As a Constituent Of The Nup107-160 Complexmentioning

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Entire Nup107-160 Complex, Including Three New Members, Is Targeted as One Entity to Kinetochores in Mitosis

Loïodice

Alves

Rabut

et al. 2004

MBoC

254

240

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“…Thus, protein import was not noticeably diminished. This suggested that Gle2p is specifically required for a NPC export func- (Wente and Blobel, 1993;Bogerd et al, 1994;Doye et al, 1994;Aitchison et al, 1995a;Gorsch et al, 1995;Heath et al, 1995;Li et al, 1995;Goldstein et al, 1996;Siniossoglou et al, 1996).…”

Section: Gle2 Is Required For Poly(a)+ Rna Exportmentioning

confidence: 99%

“…Mutations in NUP145 (Wente and Blobel, 1994), NUP133 (Doye et al, 1994;Li et al, 1995;Pemberton et al, 1995), NUP120 (Aitchison et al, 1995a;Heath et al, 1995), NUP159 (Gorsch et al, 1995), NUP84 (Siniossoglou et al, 1996), and NUP85 (Goldstein et al, 1996;Siniossoglou et al, 1996) (Figure 6, right). The same was true for gle2 cells grown at 23°C (igure 6, top left).…”

Section: Gle2 Is Required For Poly(a)+ Rna Exportmentioning

confidence: 99%

GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function.

Murphy

Watkins

Wente

1996

MBoC

168

164

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To identify and characterize novel factors required for nuclear transport, a genetic screen was conducted in the yeast Saccharomyces cerevisiae. Mutations that were lethal in combination with a null allele of the gene encoding the nucleoporin NuplOOp were isolated using a colony-sectoring assay. Three complementation groups of gle (for GLFG lethal) mutants were identified. In this report, the characterization of GLE2 is detailed. GLE2 encodes a 40.5-kDa polypeptide with striking similarity to that of Schizosaccharomyces pombe RAE1. In indirect immunofluorescence and nuclear pore complex fractionation experiments, Gle2p was associated with nuclear pore complexes. Mutated alleles of GLE2 displayed blockage of polyadenylated RNA export; however, nuclear protein import was not apparently diminished. Immunofluorescence and thin-section electron microscopic analysis revealed that the nuclear pore complex and nuclear envelope structure was grossly perturbed in gle2 mutants. Because the clusters of herniated pore complexes appeared subsequent to the export block, the structural perturbations were likely indirect consequences of the export phenotype. Interestingly, a two-hybrid interaction was detected between Gle2p and Srplp, the nuclear localization signal receptor, as well as Riplp, a nuclear export signal-interacting protein. We propose that Gle2p has a novel role in mediating nuclear transport.

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Sequence Analysis of 203 Kilobases fromSaccharomyces cerevisiae Chromosome VII

Rieger

Brückner

Schäfer

et al. 1997

Yeast

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The nucleotide sequences of five major regions from chromosome VII of Saccharomyces cerevisiae have been determined and analysed. These regions represent 203 kilobases corresponding to approximately one‐fifth of the complete yeast chromosome VII. Two fragments originate from the left arm of this chromosome. The first one of about 15·8 kb starts approximately 75 kb from the left telomere and is bordered by the SKI8 chromosomal marker. The second fragment covers the 72·6 kb region between the chromosomal markers CYH2 and ALG2. On the right chromosomal arm three regions, a 70·6 kb region between the MSB2 and the KSS1 chromosomal markers and two smaller regions dominated by the KRE11 marker and another one in the vicinity of the SER2 marker were sequenced. We found a total of 114 open reading frames (ORFs), 13 of which were completely overlapping with larger ORFs running in the opposite direction. A total of 44 yeast genes, the physiological functions of which are known, could be precisely mapped on this chromosome. Of the remaining 57 ORFs, 26 shared sequence homologies with known genes, among which were 13 other S. cerevisiae genes and five genes from other organisms. No homology with any sequence in the databases could be found for 31 ORFs. Furthermore, five Ty elements were found, one of which may not be functional due to a frame shift in its Ty1B amino acid sequence. The five chromosomal regions harboured five potential ARS elements and one sigma element together with eight tRNA genes and two snRNAs, one of which is encoded by an intron of a protein‐coding gene. © 1997 by John Wiley & Sons, Ltd.

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A Novel Complex of Nucleoporins, Which Includes Sec13p and a Sec13p Homolog, Is Essential for Normal Nuclear Pores

Cited by 308 publications

References 30 publications

The Entire Nup107-160 Complex, Including Three New Members, Is Targeted as One Entity to Kinetochores in Mitosis

The Entire Nup107-160 Complex, Including Three New Members, Is Targeted as One Entity to Kinetochores in Mitosis

GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function.

Sequence Analysis of 203 Kilobases fromSaccharomyces cerevisiae Chromosome VII

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