Evidence map›Paper›PMID 11259602›Full record

ArticleMolecular and cellular biology2001

NXT1 (p15) is a crucial cellular cofactor in TAP-dependent export of intron-containing RNA in mammalian cells.

B W Guzik, L Levesque, S Prasad, Y C Bor, B E Black, B M Paschal, D Rekosh, M L Hammarskjöld

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

51 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Review
  3. Unraveling docking and initiation of mRNA export through the nuclear pore complex.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  4. Distinct roles of nuclear basket proteins in directing the passage of mRNA through the nuclear pore.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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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

8 authors at 1 institution in 1 country.

B W GuzikMyles H. Thaler Center for AIDS and Human Retrovirus Research and Department of Microbiology, University of Virginia, Charlottesville, Virginia 22908, USA.
L Levesque
S Prasad
Y C Bor
B E Black
B M Paschal
D Rekosh
M L Hammarskjöld
University of Virginia · US

Funding

HIV PARTICLE FORMATION AND RNA PACKAGINGR01AI047008 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI REKOSH, DAVID M · 2000 to 2003
$1.0M
REGULATION OF HIV RNA PROCESSING AND TRANSPORTR01AI034721 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HAMMARSKJOLD, MARIE-LOUISE · 1994 to 2002
$734k
NIAID NIH HHS AI34721NIAID NIH HHS AI47008NIAID NIH HHS R01 AI047008
6 · The paper itself

Abstract

TAP, the human homologue of the yeast protein Mex67p, has been proposed to serve a role in mRNA export in mammalian cells. We have examined the ability of TAP to mediate export of Rev response element (RRE)-containing human immunodeficiency virus (HIV) RNA, a well-characterized export substrate in mammalian cells. To do this, the TAP gene was fused in frame to either RevM10 or RevDelta78-79. These proteins are nonfunctional Rev mutant proteins that can bind to HIV RNA containing the RRE in vivo but are unable to mediate the export of this RNA to the cytoplasm. However, the fusion of TAP to either of these mutant proteins gave rise to chimeric proteins that were able to complement Rev function. Significantly, cotransfection with a vector expressing NXT1 (p15), an NTF2-related cellular factor that binds to TAP, led to dramatic enhancement of the ability of the chimeric proteins to mediate RNA export. Mutant-protein analysis demonstrated that the domain necessary for nuclear export mapped to the C-terminal region of TAP and required the domain that interacts with NXT1, as well as the region that has been shown to interact with nucleoporins. RevM10-TAP function was leptomycin B insensitive. In contrast, the function of this protein was inhibited by DeltaCAN, a protein consisting of part of the FG repeat domain of CAN/Nup214. These results show that TAP can complement Rev nuclear export signal function and redirect the export of intron-containing RNA to a CRM1-independent pathway. These experiments support the role of TAP as an RNA export factor in mammalian cells. In addition, they indicate that NXT1 serves as a crucial cellular cofactor in this process.

Indexed as

Nucleocytoplasmic Transport ProteinsSaccharomyces cerevisiae ProteinsAnimalsATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 2Biological TransportCarrier ProteinsCell LineHumansIntronsMutationNuclear ProteinsRNARNA-Binding ProteinsATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 2Carrier ProteinsMEX67 protein, S cerevisiaeNuclear ProteinsNucleocytoplasmic Transport ProteinsNXT1 protein, humanRNARNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTAP1 protein, human

Identifiers

PMID11259602
PMCPMC86886
OpenAlexW2165589515

What OpenQuestion holds

Textmetadata
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.