Evidence map›Paper›PMID 11050168›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Vigilin binding selectively inhibits cleavage of the vitellogenin mRNA 3'-untranslated region by the mRNA endonuclease polysomal ribonuclease 1.

K S Cunningham, R E Dodson, M A Nagel, D J Shapiro, D R Schoenberg

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.6field-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

27 citing papers in PubMed, 85 citations in OpenAlex.

  1. The DNMT1-PAS1-PH20 axis drives breast cancer growth and metastasis.Signal transduction and targeted therapy · 2022
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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

5 authors at 2 institutions in 1 country.

K S CunninghamDepartment of Molecular and Cellular Biochemistry, The Comprehensive Cancer Center, and Ohio State Biochemistry Program, Ohio State University, Columbus, OH 43210, USA.
R E Dodson
M A Nagel
D J Shapiro
D R Schoenberg
University of Illinois Urbana-Champaign · USThe Ohio State University · US

Funding

Hormonal Regulation of mRNA StabilityR01GM038277 · NIGMS · OHIO STATE UNIVERSITY · PI SCHOENBERG, DANIEL R. · 1987 to 2013
$4.8M
ESTROGEN REGULATED MRNA BINDING PROTEIN IN RNA STABILITYR01DK050080 · NIDDK · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SHAPIRO, DAVID J · 1995 to 2004
$1.1M
NIDDK NIH HHS R01 DK050080NIGMS NIH HHS GM38277NIGMS NIH HHS R01 GM038277
6 · The paper itself

Abstract

In Xenopus, estrogen induces the stabilization of vitellogenin mRNA and the destabilization of albumin mRNA. These processes correlate with increased polysomal activity of a sequence-selective mRNA endonuclease, PMR-1, and a hnRNP K homology-domain RNA-binding protein, vigilin. Vigilin binds to a region of the vitellogenin mRNA 3'-untranslated region (3'-UTR) implicated in estrogen-mediated stabilization. The vigilin-binding site in the vitellogenin B1 mRNA 3'-UTR contains two consensus PMR-1 cleavage sites. The availability of purified PMR-1 and recombinant vigilin made it possible to test the hypothesis that RNA-binding proteins interact with cis-acting elements to stabilize target mRNAs by blocking cleavage by site-specific mRNA endonucleases. Vigilin binds to the vitellogenin mRNA 3'-UTR site with at least 30-fold higher affinity than it exhibits for the albumin mRNA segment containing the mapped PMR-1 cleavage sites. This differential binding affinity correlates with differential in vitro susceptibility of the protein-RNA complexes to cleavage by PMR-1. Whereas recombinant vigilin has no detectable protective effect on PMR-1 cleavage of albumin mRNA, it retards in vitro cleavage of the vitellogenin mRNA 3'-UTR by purified PMR-1. The PMR-1 sites in the vitellogenin mRNA 3'-UTR are functional because they are readily cleaved in vitro by purified PMR-1. These results provide direct evidence for differential susceptibility to endonuclease-mediated mRNA decay resulting from the differential affinity of a RNA-binding protein for cis-acting stability determinants.

Indexed as

Carrier Proteins3' Untranslated RegionsAnimalsBase SequenceCell LineEndoribonucleasesHumansMaleMolecular Sequence DataNucleic Acid ConformationRecombinant Fusion ProteinsRNA-Binding ProteinsSpodopteraSubstrate SpecificityVitellogeninsXenopus3' Untranslated RegionsCarrier ProteinsEndoribonucleaseshigh density lipoprotein binding proteinpolysomal RNase 1Recombinant Fusion ProteinsRNA-Binding ProteinsVitellogenins

Identifiers

PMID11050168
PMCPMC18792
OpenAlexW2086727856

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.