Evidence map›Paper›PMID 20144953›Full record

ArticleNucleic acids research2010

Targeting of the cytosolic poly(A) binding protein PABPC1 to mitochondria causes mitochondrial translation inhibition.

Mateusz Wydro, Agnieszka Bobrowicz, Richard J Temperley, Robert N Lightowlers, Zofia M Chrzanowska-Lightowlers

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Human Mitochondrial RNA Processing and Modifications: Overview.International journal of molecular sciences · 2021
    Review
  3. Article
  4. Mechanisms and regulation of protein synthesis in mitochondria.Nature reviews. Molecular cell biology · 2021
    Review
  5. Article
  6. Review
  7. Review
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  15. Article
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  17. Article
  18. Mitochondrial transcript maturation and its disorders.Journal of inherited metabolic disease · 2015
    Review
  19. Review
  20. 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

5 authors at 2 institutions in 1 country.

Mateusz WydroMitochondrial Research Group, Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, UK.
Agnieszka Bobrowicz
Richard J Temperley
Robert N Lightowlers
Zofia M Chrzanowska-Lightowlers
Wellcome Centre for Mitochondrial Research · GBNewcastle University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F011520/1Medical Research Council G0700718Wellcome Trust 074454Wellcome Trust 074454/Z/04/Z
6 · The paper itself

Abstract

Mammalian mitochondria contain their own genome that is almost fully transcribed from both strands, generating polycistronic RNA units that are processed and matured. The mitochondrial mRNA is modified by oligo- or polyadenylation at the 3' termini, but the exact function of this post-transcriptional addition is unclear. Current debate focuses on the role of polyadenylation in transcript stability. An equally likely function that has received little attention is that, as in the cytosol of eukaryotes, polyadenylation facilitates translation in the mitochondrion. To address this issue, we have targeted cytosolic proteins to the mitochondrion, a poly(A) specific 3' exoribonuclease, mtPARN, and a poly(A)binding protein, mtPABP1. Removal of the 3' adenylyl extensions had a variable effect on mt-mRNA steady-state levels, increasing (MTND1, 2, 5) or decreasing (MTCO1, 2, RNA14) certain species with minimal effect on others (RNA7, MTND3). Translation was markedly affected, but interpretation of this was complicated by the concomitant 3' truncation of the open reading frame in most cases. Coating of the poly(A) tail by mtPABP1, however, did not lead to transcript decay but caused a marked inhibition of mitochondrial translation. These data are consistent with endogenous RNA-binding factor(s) interacting with the poly(A) to optimize mitochondrial protein synthesis.

Indexed as

Protein BiosynthesisCell LineElectron Transport Chain Complex ProteinsExoribonucleasesHumansMitochondriaMitochondrial ProteinsPhenotypePoly APoly(A)-Binding Protein IProtein TransportRNARNA, MessengerRNA, MitochondrialRNA StabilityElectron Transport Chain Complex ProteinsExoribonucleasesMitochondrial ProteinsPoly APoly(A)-Binding Protein IRNARNA, MessengerRNA, Mitochondrial

Identifiers

PMID20144953
PMCPMC2887948
OpenAlexW2024356064

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.