Evidence map›Paper›PMID 20543818›Full record

ArticleThe EMBO journal2010

The C-terminal alpha-alpha superhelix of Pat is required for mRNA decapping in metazoa.

Joerg E Braun, Felix Tritschler, Gabrielle Haas, Cátia Igreja, Vincent Truffault, Oliver Weichenrieder, Elisa Izaurralde

Abstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

  1. Article
  2. Novel Genetic Variants inInternational journal of medical sciences · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. DNA topoisomerase 2-associated proteins PATL1 and PATL2 regulate the biogenesis of hERG KProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  11. Article
  12. Pat1 activates late steps in mRNA decay by multiple mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. mRNA decapping: finding the right structures.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  17. Article
  18. A unique surface on Pat1 C-terminal domain directly interacts with Dcp2 decapping enzyme and Xrn1 5'-3' mRNA exonuclease in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. 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

7 authors.

Joerg E BraunDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Felix Tritschler
Gabrielle Haas
Cátia Igreja
Vincent Truffault
Oliver Weichenrieder
Elisa Izaurralde

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pat proteins regulate the transition of mRNAs from a state that is translationally active to one that is repressed, committing targeted mRNAs to degradation. Pat proteins contain a conserved N-terminal sequence, a proline-rich region, a Mid domain and a C-terminal domain (Pat-C). We show that Pat-C is essential for the interaction with mRNA decapping factors (i.e. DCP2, EDC4 and LSm1-7), whereas the P-rich region and Mid domain have distinct functions in modulating these interactions. DCP2 and EDC4 binding is enhanced by the P-rich region and does not require LSm1-7. LSm1-7 binding is assisted by the Mid domain and is reduced by the P-rich region. Structural analysis revealed that Pat-C folds into an alpha-alpha superhelix, exposing conserved and basic residues on one side of the domain. This conserved and basic surface is required for RNA, DCP2, EDC4 and LSm1-7 binding. The multiplicity of interactions mediated by Pat-C suggests that certain of these interactions are mutually exclusive and, therefore, that Pat proteins switch decapping partners allowing transitions between sequential steps in the mRNA decapping pathway.

Indexed as

Protein Structure, TertiaryAmino Acid SequenceAnimalsCell LineDNA-Binding ProteinsDrosophila melanogasterHumansModels, MolecularMolecular Sequence DataMutationProtein FoldingRecombinant Fusion ProteinsRNA-Binding ProteinsRNA CapsRNA, MessengerSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsPAT1 protein, S cerevisiaePATL1 protein, humanRecombinant Fusion ProteinsRNA-Binding ProteinsRNA CapsRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID20543818
PMCPMC2910274

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Registered trials

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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.