Evidence map›Paper›PMID 22203041›Full record

ArticleMolecular and cellular biology2012

AU-rich-element-dependent translation repression requires the cooperation of tristetraprolin and RCK/P54.

Mei-Yan Qi, Zhi-Zhang Wang, Zhuo Zhang, Qin Shao, An Zeng, Xiang-Qi Li, Wen-Qing Li, Chen Wang, Fu-Ju Tian, Qing Li and 5 more

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.6field-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

47 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
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  10. Overview of RAW264.7 for osteoclastogensis study: Phenotype and stimuli.Journal of cellular and molecular medicine · 2019
    Review
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  17. Targeting RNA helicases in cancer: The translation trap.Biochimica et biophysica acta. Reviews on cancer · 2017
    Review
  18. Article
  19. 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

15 authors at 6 institutions in 2 countries.

Mei-Yan QiKey Laboratory of Stem Cell Biology, Institute of Health Sciences, Shanghai Institutes for Biological Sciences, Graduate School of Chinese Academy of Sciences & Shanghai Jiao-Tong University School of Medicine, Shanghai, China.
Zhi-Zhang Wang
Zhuo Zhang
Qin Shao
An Zeng
Xiang-Qi Li
Wen-Qing Li
Chen Wang
Fu-Ju Tian
Qing Li
Jun Zou
Yong-Wen Qin
Gary Brewer
Shuang Huang
Qing Jing
Shanghai Institutes for Biological Sciences · CNChanghai Hospital · CNChinese Academy of Sciences · CNSecond Military Medical University · CNJohnson University · USShanghai Jiao Tong University · CN

Funding

POST TRANSCRIPTIONAL REGULATION--ONCOGENE MESSENGER RNAR01CA052443 · NCI · WAKE FOREST UNIVERSITY · PI BREWER, GARY A. · 1990 to 2012
$4.3M
NCI NIH HHS CA052443NCI NIH HHS R01 CA052443
6 · The paper itself

Abstract

AU-rich elements (AREs), residing in the 3' untranslated region (UTR) of many labile mRNAs, are important cis-acting elements that modulate the stability of these mRNAs by collaborating with trans-acting factors such as tristetraprolin (TTP). AREs also regulate translation, but the underlying mechanism is not fully understood. Here we examined the function and mechanism of TTP in ARE-mRNA translation. Through a luciferase-based reporter system, we used knockdown, overexpression, and tethering assays in 293T cells to demonstrate that TTP represses ARE reporter mRNA translation. Polyribosome fractionation experiments showed that TTP shifts target mRNAs to lighter fractions. In murine RAW264.7 macrophages, knocking down TTP produces significantly more tumor necrosis factor alpha (TNF-α) than the control, while the corresponding mRNA level has a marginal change. Furthermore, knockdown of TTP increases the rate of biosynthesis of TNF-α, suggesting that TTP can exert effects at translational levels. Finally, we demonstrate that the general translational repressor RCK may cooperate with TTP to regulate ARE-mRNA translation. Collectively, our studies reveal a novel function of TTP in repressing ARE-mRNA translation and that RCK is a functional partner of TTP in promoting TTP-mediated translational repression.

Indexed as

DEAD-box RNA HelicasesProtein BiosynthesisProto-Oncogene ProteinsTristetraprolin3' Untranslated RegionsAnimalsCell LineHumansMacrophagesMiceRegulatory Sequences, Nucleic AcidRNA, MessengerTumor Necrosis Factor-alpha3' Untranslated RegionsDDX6 protein, humanDdx6 protein, mouseDEAD-box RNA HelicasesProto-Oncogene ProteinsRNA, MessengerTristetraprolinTumor Necrosis Factor-alpha

Identifiers

PMID22203041
PMCPMC3295194
OpenAlexW1980506695

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.