Evidence map›Paper›PMID 18562319›Full record

ArticleThe Journal of biological chemistry2008

Heterogeneous nuclear ribonucleoprotein A1 regulates cyclin D1 and c-myc internal ribosome entry site function through Akt signaling.

Oak D Jo, Jheralyn Martin, Andrew Bernath, Janine Masri, Alan Lichtenstein, Joseph Gera

Erratum issuedOpen 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. An erratum has been issued. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

82 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Article
  3. IRES-Mediated Translation: Expanding the Toolkits of RNA Therapy.International journal of molecular sciences · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. mCancer letters · 2023
    Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

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

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Oak D JoDepartment of Research and Development, Greater Los Angeles Veterans Affairs Healthcare System, Los Angeles, California 91343, USA.
Jheralyn Martin
Andrew Bernath
Janine Masri
Alan Lichtenstein
Joseph Gera
VA Greater Los Angeles Healthcare System · USUniversity of California, Los Angeles · US

Funding

Women's CancersP30CA016042 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Melissa Fitzmaurice Neligan · 1985 to 2026
$134.5M
Virology CoreP30AI028697 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MITSUYASU, RONALD T. · 1991 to 2018
$39.9M
Sensitivity of multiple myeloma cells to mTOR inhibitorsR01CA111448 · NCI · BRENTWOOD BIOMEDICAL RESEARCH INSTITUTE · PI LICHTENSTEIN, ALAN K · 2005 to 2016
$1.9M
Mechanisms of AKT-dependent sensitivity to rapamycinR01CA109312 · NCI · SEPULVEDA RESEARCH CORPORATION · PI GERA, JOSEPH F · 2005 to 2012
$1.6M
NCI NIH HHS CA-16042NCI NIH HHS P30 CA016042NCI NIH HHS R01CA109312NCI NIH HHS R01CA111448NIAID NIH HHS AI-28697NIAID NIH HHS P30 AI028697
6 · The paper itself

Abstract

The translation of the cyclin D1 and c-myc mRNAs occurs via internal ribosome entry site (IRES)-mediated initiation under conditions of reduced eIF-4F complex formation and Akt activity. Here we identify hnRNP A1 as an IRES trans-acting factor that regulates cyclin D1 and c-myc IRES activity, depending on the Akt status of the cell. hnRNP A1 binds both IRESs in vitro and in intact cells and enhances in vitro IRES-dependent reporter expression. Akt regulates this IRES activity by inducing phosphorylation of hnRNP A1 on serine 199. Serine 199-phosphorylated hnRNP A1 binds to the IRESs normally but is unable to support IRES activity in vitro. Reducing expression levels of hnRNP A1 or overexpressing a dominant negative version of the protein markedly inhibits rapamycin-stimulated IRES activity in cells and correlated with redistribution of cyclin D1 and c-myc transcripts from heavy polysomes to monosomes. Importantly, knockdown of hnRNP A1 also renders quiescent Akt-containing cells sensitive to rapamycin-induced G(1) arrest. These results support a role for hnRNP A1 in mediating rapamycin-induced alterations of cyclin D1 and c-myc IRES activity in an Akt-dependent manner and provide the first direct link between Akt and the regulation of IRES activity.

Indexed as

AnimalsAntibiotics, AntineoplasticBinding SitesCell LineCell Line, TumorCyclin D1Heterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHumansMicePhosphorylationProto-Oncogene Proteins c-aktProto-Oncogene Proteins c-mycRibosomesSerineSirolimusAntibiotics, AntineoplasticCyclin D1Heterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BhnRNPA1 protein, humanHnrnpa1 protein, mouseProto-Oncogene Proteins c-aktProto-Oncogene Proteins c-mycSerineSirolimus

Identifiers

PMID18562319
PMCPMC2516998
OpenAlexW2048962172

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.