Evidence map›Paper›PMID 16556936›Full record

ArticleRNA (New York, N.Y.)2006

Assembly of AUF1 with eIF4G-poly(A) binding protein complex suggests a translation function in AU-rich mRNA decay.

Jin-Yu Lu, Naomi Bergman, Navid Sadri, Robert J Schneider

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

48 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
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  11. AUF1 regulation of coding and noncoding RNA.Wiley interdisciplinary reviews. RNA · 2017
    Review
  12. Review
  13. Article
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  17. Review
  18. Review
  19. Article
  20. Translation initiation mediated by RNA looping.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
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

4 authors at 2 institutions in 1 country.

Jin-Yu LuDepartment of Microbiology, New York University School of Medicine, New York, New York 10016, USA.
Naomi Bergman
Navid Sadri
Robert J Schneider
Howard Hughes Medical Institute · USNew York University · US

Funding

Control of Cytoxine mRNA Stability by AUF1R01GM060428 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SCHNEIDER, ROBERT · 2000 to 2007
$2.4M
NIGMS NIH HHS GM60428NIGMS NIH HHS R01 GM060428
6 · The paper itself

Abstract

An AU-rich element (ARE) located in the 3'-untranslated region of many short-lived mRNAs functions as an instability determinant for these transcripts. AUF1/hnRNP D, an ARE-binding protein family consisting of four isoforms, promotes rapid decay of ARE-mRNAs. The mechanism by which AUF1 promotes rapid decay of ARE-mRNA is unclear. AUF1 has been shown to form an RNase-resistant complex in cells with the cap-initiation complex and heat shock proteins Hsp70 and Hsc70, as well as other unidentified factors. To understand the function of the AUF1 complex, we have biochemically investigated the association of AUF1 with the components of the translation initiation complex. We used purified recombinant proteins and a synthetic ARE RNA oligonucleotide to determine the hierarchy of protein interactions in vitro and the effect of AUF1 binding to the ARE on the formation of protein complexes. We demonstrate that all four AUF1 protein isoforms bind directly and strongly to initiation factor eIF4G at a C-terminal site regardless of AUF1 interaction with the ARE. AUF1 is shown to directly interact with poly(A) binding protein (PABP), both independently of eIF4G and in a complex with eIF4G. AUF1-PABP interaction is opposed by AUF1 binding to the ARE or Hsp70 heat shock protein. In vivo, AUF1 interaction with PABP does not alter PABP stability. Based on these and other data, we propose a model for the molecular interactions of AUF1 that involves translation-dependent displacement of AUF1-PABP complexes from ARE-mRNAs with possible unmasking of the poly(A) tail.

Indexed as

Protein Biosynthesis3' Untranslated RegionsAnimalsBinding SitesCHO CellsCricetinaeEukaryotic Initiation Factor-4GGlutathione TransferaseHeterogeneous-Nuclear Ribonucleoprotein DHeterogeneous Nuclear Ribonucleoprotein D0HistidineHSP70 Heat-Shock ProteinsIn Vitro TechniquesPoly(A)-Binding ProteinsProtein BindingProtein Isoforms3' Untranslated RegionsEukaryotic Initiation Factor-4GGlutathione TransferaseHeterogeneous-Nuclear Ribonucleoprotein DHeterogeneous Nuclear Ribonucleoprotein D0HistidineHSP70 Heat-Shock ProteinsPoly(A)-Binding ProteinsProtein IsoformsProtein Synthesis InhibitorsRecombinant Fusion ProteinsRNA, Messenger

Identifiers

PMID16556936
PMCPMC1440908
OpenAlexW2139911809

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.