Evidence map›Paper›PMID 22357952›Full record

ArticleJournal of cell science2012

Association of translation factor eEF1A with defective ribosomal products generates a signal for aggresome formation.

Anatoli B Meriin, Nava Zaarur, Michael Y Sherman

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 39 citations in OpenAlex.

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  12. Hsp70-Bag3 complex is a hub for proteotoxicity-induced signaling that controls protein aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2018
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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

3 authors at 1 institution in 1 country.

Anatoli B MeriinDepartment of Biochemistry, Boston University Medical School, Boston, MA 02118, USA.
Nava Zaarur
Michael Y Sherman
Boston University · US

Funding

Cellular Mechanisms of Aggregation of Abnormal ProteinsR01GM086890 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SHERMAN, MICHAEL Y · 2009 to 2012
$1.5M
NIGMS NIH HHS R01 GM086890NIGMS NIH HHS R01GM086890
6 · The paper itself

Abstract

Aggresome formation is initiated upon proteasome failure, and facilitates autophagic clearance of protein aggregates to protect cells from proteotoxicity. Here we demonstrate that proteasome inhibition generates a signaling event to trigger aggresome formation. In aggresome signaling, the cell senses a build-up of aberrant newly synthesized proteins. The translation elongation factor eEF1A associated with these species, and knockdown of this factor suppressed aggresome formation. We used the Legionella toxin SidI to distinguish between the function of eEF1A in translation and its novel function in the aggresome formation. In fact, although it strongly inhibited translation, this toxin had only a marginal effect on aggresome formation. Furthermore, SidI reduced the threshold of the aberrant ribosomal products for triggering aggresome formation. Therefore, eEF1A binds defective polypeptides released from ribosomes, which generates a signal that triggers aggresome formation.

Indexed as

Protein BiosynthesisSignal TransductionHeLa CellsHumansInclusion BodiesPeptide Elongation Factor 1Protein BindingProtein Synthesis InhibitorsRibosomesToxins, BiologicalEEF1A1 protein, humanPeptide Elongation Factor 1Protein Synthesis InhibitorsToxins, Biological

Identifiers

PMID22357952
PMCPMC3403235
OpenAlexW2128912255

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.