Evidence map›Paper›PMID 18682389›Full record

ArticleThe Journal of biological chemistry2008

Functional significance of the interaction between the mRNA-binding protein, Nab2, and the nuclear pore-associated protein, Mlp1, in mRNA export.

Milo B Fasken, Murray Stewart, Anita H Corbett

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

60 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. The Molecular Architecture of the Nuclear Basket.bioRxiv : the preprint server for biology · 2024
    Article
  13. Article
  14. The Great Escape: mRNA Export through the Nuclear Pore Complex.International journal of molecular sciences · 2021
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Polyadenylation and nuclear export of mRNAs.The Journal of biological chemistry · 2019
    Review
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

3 authors at 2 institutions in 2 countries.

Milo B FaskenDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
Murray Stewart
Anita H Corbett
Emory University · USMRC Laboratory of Molecular Biology · GB

Funding

MOLECULAR BASIS OF RAN MEDIATED NUCLEAR TRANSPORTR01GM058728 · NIGMS · EMORY UNIVERSITY · PI CORBETT, ANITA H. · 1999 to 2016
$5.4M
Medical Research Council MC_U105178939NIGMS NIH HHS R01 GM058728Wellcome Trust
6 · The paper itself

Abstract

Nuclear export of mRNA requires several key mRNA-binding proteins that recognize and remodel the mRNA and target it for export via interactions with the nuclear pore complex. In Saccharomyces cerevisiae, the shuttling heterogeneous nuclear ribonucleoprotein, Nab2, which is essential for mRNA export, specifically recognizes poly(A) RNA and binds to the nuclear pore-associated protein, myosin-like protein 1 (Mlp1), which functions in mRNA export and quality control. Specifically, the N-terminal domain of Nab2 (Nab2-N; residues 1-97) interacts directly with the C-terminal globular domain of Mlp1 (CT-Mlp1: residues 1490-1875). Recent structural and binding studies focused on Nab2-N have shown that Nab2-N contains a hydrophobic patch centered on Phe(73) that is critical for interaction with Mlp1. Engineered amino acid changes within this patch disrupt the Nab2/Mlp1 interaction in vitro. Given the importance of Nab2 and Mlp1 to mRNA export, we have examined the Nab2/Mlp1 interaction in greater detail and analyzed the functional consequences of disrupting the interaction in vivo. We find that the Nab2-binding domain of Mlp1 (Mlp1-NBD) maps to a 183-residue region (residues 1586-1768) within CT-Mlp1, binds directly to Nab2 with micromolar affinity, and confers nuclear accumulation of poly(A) RNA. Furthermore, we show that cells expressing a Nab2 F73D mutant that cannot interact with Mlp1 exhibit nuclear accumulation of poly(A) RNA and that this nab2 F73D mutant genetically interacts with alleles of two essential mRNA export genes, MEX67 and YRA1. These data provide in vivo evidence for a model of mRNA export in which Nab2 is important for targeting mRNAs to the nuclear pore for export.

Indexed as

Active Transport, Cell NucleusAmino Acid SubstitutionNuclear PoreNuclear ProteinsNucleocytoplasmic Transport ProteinsPoly AProtein Structure, TertiaryRNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMEX67 protein, S cerevisiaeMLP1 protein, S cerevisiaeNAB2 protein, S cerevisiaeNuclear ProteinsNucleocytoplasmic Transport ProteinsPoly ARNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsYRA1 protein, S cerevisiae

Identifiers

PMID18682389
PMCPMC2555995
OpenAlexW2066377184

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.