Evidence map›Paper›PMID 35264577›Full record

ArticleNature communications2022

Co-translational assembly orchestrates competing biogenesis pathways.

Maximilian Seidel, Anja Becker, Filipa Pereira, Jonathan J M Landry, Nayara Trevisan Doimo de Azevedo, Claudia M Fusco, Eva Kaindl, Natalie Romanov, Janina Baumbach, Julian D Langer and 5 more

Abstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Cotranslational assembly directs the biogenesis of the mProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  6. 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
    Article
  7. Article
  8. Article
  9. Review
  10. 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
  11. YTHDF1 is pivotal for maintenance of cardiac homeostasis.Journal of molecular and cellular cardiology · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Benefits of co-translational complex assembly for cellular fitness.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  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

15 authors.

Maximilian SeidelDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID http://orcid.org/0000-0003-1615-3549
Anja BeckerDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Frankfurt, Germany.
Filipa PereiraStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Jonathan J M LandryGenomics Core Facility, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Nayara Trevisan Doimo de AzevedoGenomics Core Facility, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Claudia M FuscoDepartment of Synaptic Plasticity, Max Planck Institute for Brain Research, Frankfurt, Germany.ORCID http://orcid.org/0000-0002-9812-2203
Eva KaindlDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Frankfurt, Germany.
Natalie RomanovDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Frankfurt, Germany.
Janina BaumbachDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Frankfurt, Germany.
Julian D LangerDepartment of Synaptic Plasticity, Max Planck Institute for Brain Research, Frankfurt, Germany.ORCID http://orcid.org/0000-0002-5190-577X
Erin M SchumanDepartment of Synaptic Plasticity, Max Planck Institute for Brain Research, Frankfurt, Germany.ORCID http://orcid.org/0000-0001-7505-1855
Kiran Raosaheb PatilStructural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Gerhard HummerDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID http://orcid.org/0000-0001-7768-746X
Vladimir BenesGenomics Core Facility, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID http://orcid.org/0000-0002-0352-2547
Martin BeckDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Frankfurt, Germany. martin.beck@biophys.mpg.de.ORCID http://orcid.org/0000-0002-7397-1321

Funding

Medical Research Council MC_UU_00025/11
6 · The paper itself

Abstract

During the co-translational assembly of protein complexes, a fully synthesized subunit engages with the nascent chain of a newly synthesized interaction partner. Such events are thought to contribute to productive assembly, but their exact physiological relevance remains underexplored. Here, we examine structural motifs contained in nucleoporins for their potential to facilitate co-translational assembly. We experimentally test candidate structural motifs and identify several previously unknown co-translational interactions. We demonstrate by selective ribosome profiling that domain invasion motifs of beta-propellers, coiled-coils, and short linear motifs may act as co-translational assembly domains. Such motifs are often contained in proteins that are members of multiple complexes (moonlighters) and engage with closely related paralogs. Surprisingly, moonlighters and paralogs assemble co-translationally in only some but not all of the relevant biogenesis pathways. Our results highlight the regulatory complexity of assembly pathways.

Indexed as

ProteinsRibosomesProtein BiosynthesisProtein DomainsProteins

Identifiers

PMID35264577
PMCPMC8907234

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.