Evidence map›Paper›PMID 10421639›Full record

ArticleGenes & development1999

Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element.

P Loflin, C Y Chen, A B Shyu

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 136 papers.

0numbers the graph read from it
0cells of the map it votes in
136citing 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

136 citing papers in PubMed, 294 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Let It Go: HIV-1Journal of virology · 2021
    Review
  7. Article
  8. Review
  9. Review
  10. Pinning Down the Transcription: A Role for Peptidyl-ProlylFrontiers in cell and developmental biology · 2020
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. RNA Degradation in Neurodegenerative Disease.Advances in neurobiology · 2018
    Review
  16. Review
  17. Translating the Untranslated Region.Journal of immunology (Baltimore, Md. : 1950) · 2015
    Review
  18. Review
  19. Article
  20. Article

76 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

P LoflinDepartment of Biochemistry and Molecular Biology, The University of Texas Houston Health Science Center, Medical School, Houston, Texas 77030 USA.
C Y Chen
A B Shyu
The University of Texas Health Science Center at Houston · US

Funding

Messenger RNA Turnover in Mammalian CellsR01GM046454 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI SHYU, ANN-BIN · 1991 to 2016
$7.1M
NIGMS NIH HHS R01 GM046454NIGMS NIH HHS R01 GM 46454
6 · The paper itself

Abstract

AU-rich RNA-destabilizing elements (AREs) have become a paradigm for studying cytoplasmic mRNA turnover in mammalian cells. Though many RNA-binding proteins have been shown to bind to AREs in vitro, trans-acting factors that participate in the in vivo destabilization of cytoplasmic RNA by AREs remains unknown. Experiments were performed to investigate the cellular mechanisms and to identify potential trans-acting factors for ARE-directed mRNA decay. These experiments identified hnRNP D, a heterogeneous nuclear ribonucleoprotein (hnRNP) capable of shuttling between the nucleus and cytoplasm, as an RNA destabilizing protein in vivo in ARE-mediated rapid mRNA decay. Our results show that the ARE destabilizing function is dramatically impeded during hemin-induced erythroid differentiation and not in TPA-induced megakaryocytic differentiation of human erythroleukemic K562 cells. A sequestration of hnRNP D into a hemin-induced protein complex, termed hemin-regulated factor or HRF, correlates well with the loss of ARE-destabilizing function in the cytoplasm. Further experiments show that in hemin-treated cells, ectopic expression of hnRNP D restores the rapid decay directed by the ARE. The extent of destabilizing effect varies among the four isoforms of hnRNP D, with p37 and p42 displaying the most profound effect. These results demonstrate a specific cytoplasmic function for hnRNP D as an RNA-destabilizing protein in ARE-mediated decay pathway. These in vivo findings support an emerging idea that shuttling hnRNP proteins have not only a nuclear but also a cytoplasmic function in mRNA metabolism. The data further imply that shuttling hnRNP proteins define, at least in part, the nuclear history of individual mRNAs and thereby influence their cytoplasmic fate.

Indexed as

Cell DifferentiationCell NucleusCytoplasmErythrocytesHeminHeterogeneous-Nuclear RibonucleoproteinsHumansK562 CellsProtein BindingRibonucleoproteinsRNA, Heterogeneous NuclearRNA, MessengerHeminHeterogeneous-Nuclear RibonucleoproteinsRibonucleoproteinsRNA, Heterogeneous NuclearRNA, Messenger

Identifiers

PMID10421639
PMCPMC316883
OpenAlexW2167635085

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.