Evidence map›Paper›PMID 10938110›Full record

ArticleMolecular and cellular biology2000

The poly(A)-binding protein and an mRNA stability protein jointly regulate an endoribonuclease activity.

Z Wang, M Kiledjian

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

50 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Article
  3. Localized 2'-OH Acylation at Poly(A) Extends RNA Translation.Journal of the American Chemical Society · 2025
    Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Advances in COVID-19 mRNA vaccine development.Signal transduction and targeted therapy · 2022
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

2 authors at 1 institution in 2 countries.

Z WangDepartment of Cell Biology and Neuroscience, Rutgers University, Piscataway, New Jersey 08854-8082, USA.
M Kiledjian
Rutgers, The State University of New Jersey · US

Funding

RNA/PROTEIN INTERACTIONS REGULATING MRNA STABILITYR01DK051611 · NIDDK · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI KILEDJIAN, MEGERDITCH · 1997 to 2006
$1.8M
NIDDK NIH HHS DK51611NIDDK NIH HHS R01 DK051611
6 · The paper itself

Abstract

We previously identified a sequence-specific erythroid cell-enriched endoribonuclease (ErEN) activity involved in the turnover of the stable alpha-globin mRNA. We now demonstrate that ErEN activity is regulated by the poly(A) tail. The unadenylated alpha-globin 3' untranslated region (3'UTR) was an efficient substrate for ErEN cleavage, while the polyadenylated 3'UTR was inefficiently cleaved in an in vitro decay assay. The influence of the poly(A) tail was mediated through the poly(A)-binding protein (PABP) bound to the poly(A) tail, which can inhibit ErEN activity. ErEN cleavage of an adenylated alpha-globin 3'UTR was accentuated upon depletion of PABP from the cytosolic extract, while addition of recombinant PABP reestablished the inhibition of endoribonuclease cleavage. PABP inhibited ErEN activity indirectly through an interaction with the alphaCP mRNA stability protein. Sequestration of alphaCP resulted in an increase of ErEN cleavage activity, regardless of the polyadenylation state of the RNA. Using electrophoretic mobility shift assays, PABP was shown to enhance the binding efficiency of alphaCP to the alpha-globin 3'UTR, which in turn protected the ErEN target sequence. Conversely, the binding of PABP to the poly(A) tail was also augmented by alphaCP, implying that a stable higher-order structural network is involved in stabilization of the alpha-globin mRNA. Upon deadenylation, the interaction of PABP with alphaCP would be disrupted, rendering the alpha-globin 3'UTR more susceptible to endoribonuclease cleavage. The data demonstrated a specific role for PABP in protecting the body of an mRNA in addition to demonstrating PABP's well-characterized effect of stabilizing the poly(A) tail.

Indexed as

Heterogeneous-Nuclear Ribonucleoproteins3' Untranslated RegionsAnimalsCytosineDNA-Binding ProteinsDose-Response Relationship, DrugEndoribonucleasesErythroid Precursor CellsGlobinsHumansMicePlasmidsPoly APoly(A)-Binding ProteinsProtein BindingRecombinant Proteins3' Untranslated RegionsCytosineDNA-Binding ProteinsEndoribonucleasesGlobinsHeterogeneous-Nuclear RibonucleoproteinsPCBP1 protein, humanPoly APoly(A)-Binding ProteinsRecombinant ProteinsRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID10938110
PMCPMC86108
OpenAlexW2158537780

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.