Evidence map›Paper›PMID 8522578›Full record

ArticleThe Journal of cell biology1995

Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p.

J D Aitchison, M P Rout, M Marelli, G Blobel, R W Wozniak

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Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
6.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

113 citing papers in PubMed, 181 citations in OpenAlex.

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  16. Shaping the nucleus: factors and forces.Journal of cellular biochemistry · 2012
    Review
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53 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

J D AitchisonLaboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York 10021, USA.
M P Rout
M Marelli
G Blobel
R W Wozniak
Howard Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have taken a combined genetic and biochemical approach to identify major constituents of the yeast nuclear pore complex (NPC). A synthetic lethal screen was used to identify proteins which interact genetically with the major pore-membrane protein Pom152p. In parallel, polypeptides present in similar amounts to Pom152p in a highly enriched preparation of yeast NPCs have been characterized by direct microsequencing. These approaches have led to the identification of two novel and major nucleoporins, Nup170p and Nup157p. Both Nup170p and Nup157p are similar to each other and to an abundant mammalian nucleoporin, Nup155p (Radu, A., G. Blobel, and R. W. Wozniak. 1993. J. Cell Biol. 121: 1-9) and interestingly, nup170 mutants can be complemented with mammalian NUP155. In addition, the synthetic lethal screen identified genetic interactions between Pom152p and two other major nucleoporins, Nup188p (Nehrbass, U., S. Maguire, M. Rout, G. Blobel, and R. W. Wozniak, manuscript submitted for publication), and Nic96p (Grandi, P., V. Doye, and E. C. Hurt. 1993. EMBO J. 12: 3061-71). We have determined that together, Nup170p, Nup157p, Pom152p, Nup188p, and Nic96p comprise greater than one-fifth of the mass of the isolated yeast NPC. Examination of the genetic interactions between these proteins indicate that while deletion of either POM152, NUP170, or NUP188 alone is not lethal, pairwise combinations are. Deletion of NUP157 is also not lethal. However, nup157 null mutants, while lethal in combination with nup170 and nup188 null alleles, are not synthetically lethal with pom152 null alleles. We suggest that Nup170p and Nup157p may be part of a morphologically symmetrical but functionally distinct substructure of the yeast NPC, e.g., the nucleoplasmic and cytoplasmic rings. Finally, we observed morphological abnormalities in the nuclear envelope as a function of alterations in the expression levels of NUP170 suggesting a specific stoichiometric relationship between NPC components is required for the maintenance of normal nuclear structure.

Indexed as

Nuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsBase SequenceDNA PrimersFluorescent Antibody Technique, IndirectFungal ProteinsGene DeletionGenetic Complementation TestMembrane GlycoproteinsMembrane ProteinsMolecular Sequence DataNuclear PoreNuclear ProteinsRatsDNA PrimersFungal ProteinsMembrane GlycoproteinsMembrane ProteinsNuclear Pore Complex ProteinsNuclear ProteinsNup155 protein, ratNUP157 protein, S cerevisiaeNUP170 protein, S cerevisiaePOM152 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID8522578
PMCPMC2120632
OpenAlexW2060403740

What OpenQuestion holds

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LicenceCC BY-NC-SA
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None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.