Evidence map›Paper›PMID 25520193›Full record

ArticleNucleic acids research2015

Novel RNA chaperone domain of RNA-binding protein La is regulated by AKT phosphorylation.

Julia Kuehnert, Gunhild Sommer, Avery W Zierk, Alena Fedarovich, Alexander Brock, Dzmitry Fedarovich, Tilman Heise

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Fluorescence-Based mRNA Translation Reporter.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Article
  4. Use of tRNA-Mediated Suppression to Assess RNA Chaperone Function.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
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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

7 authors at 1 institution in 1 country.

Julia KuehnertDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.
Gunhild SommerDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.
Avery W ZierkDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.
Alena FedarovichDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.
Alexander BrockDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.
Dzmitry FedarovichDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.
Tilman HeiseDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA heise@musc.edu.
Medical University of South Carolina · US

Funding

Screen for Inhibitors of La-dependent IRES-mediated Translation in Cancer CellsR01CA172567 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI HEISE, TILMAN · 2013 to 2015
$921k
Role and Function of RNA-Binding Protein La in Oral Tumor ProgressionR03DE021729 · NIDCR · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI SOMMER, GUNHILD · 2011 to 2012
$221k
NCI NIH HHS 1R01CA172567-01A1NCI NIH HHS R01 CA172567NIDCR NIH HHS 1R03DE021729-01
6 · The paper itself

Abstract

The cellular function of the cancer-associated RNA-binding protein La has been linked to translation of viral and cellular mRNAs. Recently, we have shown that the human La protein stimulates IRES-mediated translation of the cooperative oncogene CCND1 in cervical cancer cells. However, there is little known about the underlying molecular mechanism by which La stimulates CCND1 IRES-mediated translation, and we propose that its RNA chaperone activity is required. Herein, we show that La binds close to the CCND1 start codon and demonstrate that La's RNA chaperone activity can change the folding of its binding site. We map the RNA chaperone domain (RCD) within the C-terminal region of La in close proximity to a novel AKT phosphorylation site (T389). Phosphorylation at T389 by AKT-1 strongly impairs its RNA chaperone activity. Furthermore, we demonstrate that the RCD as well as T389 is required to stimulate CCND1 IRES-mediated translation in cells. In summary, we provide a model whereby a novel interplay between RNA-binding, RNA chaperoning and AKT phosphorylation of La protein regulates CCND1 IRES-mediated translation.

Indexed as

5' Untranslated RegionsAmino Acid MotifsAutoantigensBinding SitesCodon, InitiatorCyclin D1HEK293 CellsHumansPhosphorylationProtein BiosynthesisProtein Structure, TertiaryProto-Oncogene Proteins c-aktRibonucleoproteinsRNASS-B AntigenThreonine5' Untranslated RegionsAutoantigensCodon, InitiatorCyclin D1Proto-Oncogene Proteins c-aktRibonucleoproteinsRNASS-B AntigenThreonine

Identifiers

PMID25520193
PMCPMC4288197
OpenAlexW2149613327

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.