Evidence map›Paper›PMID 11684705›Full record

ArticleThe Journal of cell biology2001

Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export.

S Vasu, S Shah, A Orjalo, M Park, W H Fischer, D J Forbes

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
3.4field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

111 citing papers in PubMed, 184 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Inactivation ofInternational journal of biological sciences · 2023
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Nucleoporins in cardiovascular disease.Journal of molecular and cellular cardiology · 2020
    Review
  17. Article
  18. Article
  19. Review
  20. Review

51 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

6 authors at 2 institutions in 1 country.

S VasuSection of Cell and Developmental Biology, Division of Biology 0347, University of California at San Diego, La Jolla, CA 92093, USA.
S Shah
A Orjalo
M Park
W H Fischer
D J Forbes
University of California, San Diego · USSalk Institute for Biological Studies · US

Funding

FUNCTIONAL STUDY OF NATIVE AND SYNTHETIC NUCLEIR01GM033279 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI FORBES, DOUGLASS JANE · 1985 to 2015
$7.0M
PROTEIN SEQUENCER SYSTEMS10RR011404 · NCRR · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI FISCHER, WOLFGANG H · 1997 to 1997
–
NCRR NIH HHS S10 RR 11404-01A1NIGMS NIH HHS R01 GM033279NIGMS NIH HHS R01 GM33279
6 · The paper itself

Abstract

RNA undergoing nuclear export first encounters the basket of the nuclear pore. Two basket proteins, Nup98 and Nup153, are essential for mRNA export, but their molecular partners within the pore are largely unknown. Because the mechanism of RNA export will be in question as long as significant vertebrate pore proteins remain undiscovered, we set out to find their partners. Fragments of Nup98 and Nup153 were used for pulldown experiments from Xenopus egg extracts, which contain abundant disassembled nuclear pores. Strikingly, Nup98 and Nup153 each bound the same four large proteins. Purification and sequence analysis revealed that two are the known vertebrate nucleoporins, Nup96 and Nup107, whereas two mapped to ORFs of unknown function. The genes encoding the novel proteins were cloned, and antibodies were produced. Immunofluorescence reveals them to be new nucleoporins, designated Nup160 and Nup133, which are accessible on the basket side of the pore. Nucleoporins Nup160, Nup133, Nup107, and Nup96 exist as a complex in Xenopus egg extracts and in assembled pores, now termed the Nup160 complex. Sec13 is prominent in Nup98 and Nup153 pulldowns, and we find it to be a member of the Nup160 complex. We have mapped the sites that are required for binding the Nup160 subcomplex, and have found that in Nup98, the binding site is used to tether Nup98 to the nucleus; in Nup153, the binding site targets Nup153 to the nuclear pore. With transfection and in vivo transport assays, we find that specific Nup160 and Nup133 fragments block poly[A]+ RNA export, but not protein import or export. These results demonstrate that two novel vertebrate nucleoporins, Nup160 and Nup133, not only interact with Nup98 and Nup153, but themselves play a role in mRNA export.

Indexed as

Nuclear ProteinsActive Transport, Cell NucleusAmino Acid SequenceAnimalsBinding SitesCell NucleusHeLa CellsHumansMiceMinor Histocompatibility AntigensMolecular Sequence DataNuclear PoreNuclear Pore Complex ProteinsPeptide FragmentsRatsRNA, MessengerMinor Histocompatibility Antigensnuclear pore complex protein 96nuclear pore complex protein 98Nuclear Pore Complex ProteinsNuclear ProteinsNUP107 protein, humanNup107 protein, ratNUP133 protein, humanNUP153 protein, humanNup153 protein, mouseNup153 protein, ratNUP160 protein, humanNup160 protein, XenopusPeptide FragmentsRNA, MessengerXenopus Proteins

Identifiers

PMID11684705
PMCPMC2150853
OpenAlexW2151126975

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

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.