Evidence map›Paper›PMID 10444597›Full record

ArticleGenes & development1999

Uncoupling of the hnRNP Npl3p from mRNAs during the stress-induced block in mRNA export.

H Krebber, T Taura, M S Lee, P A Silver

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
–field-weighted citation impact
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

42 citing papers in PubMed, 77 citations in OpenAlex.

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  11. Keeping mRNPs in check during assembly and nuclear export.Nature reviews. Molecular cell biology · 2011
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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

4 authors at 2 institutions in 1 country.

H KrebberDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and The Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.
T Taura
M S Lee
P A Silver
Dana-Farber Cancer Institute · USHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Npl3p, the major mRNA-binding protein of the yeast Saccharomyces cerevisiae shuttles between the nucleus and the cytoplasm. A single amino acid change in the carboxyl terminus of Npl3p (E409 --> K) renders the mutant protein largely cytoplasmic because of a delay in its import into the nucleus. This import defect can be reversed by increasing the intracellular concentration of Mtr10p, the nuclear import receptor for Npl3p. Conversely, using this mutant, we show that Npl3p and mRNA export out of the nucleus is significantly slowed in cells bearing mutations in XPO1/CRM1, which encodes the export receptor for NES-containing proteins and in RAT7, which encodes an essential nucleoporin. Interestingly, following induction of stress by heat shock, high salt, or ethanol, conditions under which most mRNA export is blocked, Npl3p is still exported from the nucleus. The stress-induced export of Npl3p is independent of both the activity of Xpo1p and the continued selective export of heat-shock mRNAs that occurs following stress. UV-cross-linking experiments show that Npl3p is bound to mRNA under normal conditions, but is no longer RNA associated in stressed cells. Taken together, we suggest that the uncoupling of Npl3p and possibly other mRNA-binding proteins from mRNAs in the nucleus provides a general switch that regulates mRNA export. By this model, under normal conditions Npl3p is a major component of an export-competent RNP complex. However, under conditions of stress, Npl3p no longer associates with the export complex, rendering it export incompetent and thus nuclear.

Indexed as

Heat-Shock ResponseKaryopherinsNuclear Pore Complex ProteinsNucleocytoplasmic Transport ProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae ProteinsBiological TransportCarrier ProteinsCell NucleusCytoplasmEthanolExportin 1 ProteinFungal ProteinsGene Expression Regulation, FungalGenes, FungalHeat-Shock ProteinsCarrier ProteinsEthanolExportin 1 ProteinFungal ProteinsHeat-Shock ProteinsHeterogeneous-Nuclear RibonucleoproteinsKaryopherinsMembrane ProteinsMTR10 protein, S cerevisiaeNPL3 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsNUP159 protein, S cerevisiaeNUP42 protein, S cerevisiaePoly AReceptors, Cytoplasmic and NuclearRibonucleoproteinsRNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID10444597
PMCPMC316916
OpenAlexW2132433958

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.