Evidence map›Paper›PMID 22144913›Full record

ArticlePLoS genetics2011

Widespread cotranslational formation of protein complexes.

Caia D S Duncan, Juan Mata

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing 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

69 citing papers in PubMed, 134 citations in OpenAlex.

  1. Article
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  5. A privileged ER compartment for posttranslational heteromeric assembly of an ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  9. Cotranslational molecular condensation of cochaperones and assembly factors facilitates axonemal dynein biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. JACS Au · 2024
    Article
  11. Article
  12. Pairwise biosynthesis of ion channels stabilizes excitability and mitigates arrhythmias.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  13. Article
  14. Review
  15. Article
  16. Article
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  18. Benefits of co-translational complex assembly for cellular fitness.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  19. Article
  20. mRNA interactions with disordered regions control protein activity.bioRxiv : the preprint server for biology · 2023
    Article

9 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Caia D S DuncanDepartment of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
Juan Mata
University of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G011869/1Department of Health BB/G011869/1
6 · The paper itself

Abstract

Most cellular processes are conducted by multi-protein complexes. However, little is known about how these complexes are assembled. In particular, it is not known if they are formed while one or more members of the complexes are being translated (cotranslational assembly). We took a genomic approach to address this question, by systematically identifying mRNAs associated with specific proteins. In a sample of 31 proteins from Schizosaccharomyces pombe that did not contain RNA-binding domains, we found that ∼38% copurify with mRNAs that encode interacting proteins. For example, the cyclin-dependent kinase Cdc2p associates with the rum1 and cdc18 mRNAs, which encode, respectively, an inhibitor of Cdc2p kinase activity and an essential regulator of DNA replication. Both proteins interact with Cdc2p and are key cell cycle regulators. We obtained analogous results with proteins with different structures and cellular functions (kinesins, protein kinases, transcription factors, proteasome components, etc.). We showed that copurification of a bait protein and of specific mRNAs was dependent on the presence of the proteins encoded by the interacting mRNAs and on polysomal integrity. These results indicate that these observed associations reflect the cotranslational interaction between the bait and the nascent proteins encoded by the interacting mRNAs. Therefore, we show that the cotranslational formation of protein-protein interactions is a widespread phenomenon.

Indexed as

Protein BiosynthesisCell Cycle ProteinsCyclin-Dependent KinasesDNA ReplicationMultiprotein ComplexesOligonucleotide Array Sequence AnalysisProtein BindingProtein Structure, TertiaryRNA-Binding ProteinsRNA, MessengerSchizosaccharomycesSchizosaccharomyces pombe Proteinscdc18 protein, S pombeCell Cycle ProteinsCyclin-Dependent KinasesMultiprotein ComplexesRNA-Binding ProteinsRNA, MessengerRum1 protein, S pombeSchizosaccharomyces pombe Proteins

Identifiers

PMID22144913
PMCPMC3228823
OpenAlexW1993411436

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.