Evidence map›Paper›PMID 20404111›Full record

ArticleThe Journal of cell biology2010

HPat provides a link between deadenylation and decapping in metazoa.

Gabrielle Haas, Joerg E Braun, Cátia Igreja, Felix Tritschler, Tadashi Nishihara, Elisa Izaurralde

Abstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing 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

54 citing papers in PubMed.

  1. Greatwall-Endos-PP2A/B55Open biology · 2024
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. 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
  11. Article
  12. Mechanistic Insights into MicroRNA-Mediated Gene Silencing.Cold Spring Harbor perspectives in biology · 2019
    Review
  13. Review
  14. mRNA decapping: finding the right structures.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  15. Review
  16. 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
  17. Article
  18. Translational repression of theRNA (New York, N.Y.) · 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

6 authors.

Gabrielle HaasMax Planck Institute for Developmental Biology, D-72076 Tübingen, Germany.
Joerg E Braun
Cátia Igreja
Felix Tritschler
Tadashi Nishihara
Elisa Izaurralde

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Decapping of eukaryotic messenger RNAs (mRNAs) occurs after they have undergone deadenylation, but how these processes are coordinated is poorly understood. In this study, we report that Drosophila melanogaster HPat (homologue of Pat1), a conserved decapping activator, interacts with additional decapping factors (e.g., Me31B, the LSm1-7 complex, and the decapping enzyme DCP2) and with components of the CCR4-NOT deadenylase complex. Accordingly, HPat triggers deadenylation and decapping when artificially tethered to an mRNA reporter. These activities reside, unexpectedly, in a proline-rich region. However, this region alone cannot restore decapping in cells depleted of endogenous HPat but also requires the middle (Mid) and the very C-terminal domains of HPat. We further show that the Mid and C-terminal domains mediate HPat recruitment to target mRNAs. Our results reveal an unprecedented role for the proline-rich region and the C-terminal domain of metazoan HPat in mRNA decapping and suggest that HPat is a component of the cellular mechanism that couples decapping to deadenylation in vivo.

Indexed as

Amino Acid SequenceAnimalsCells, CulturedDEAD-box RNA HelicasesDrosophila melanogasterDrosophila ProteinsEndoribonucleasesHomeodomain ProteinsHumansMolecular Sequence DataProtein Structure, TertiaryRecombinant Fusion ProteinsRibonucleasesRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA CapsCCR4 protein, DrosophilaDEAD-box RNA HelicasesDrosophila ProteinsEdc3 protein, DrosophilaEndoribonucleasesHomeodomain ProteinsLcp2 protein, DrosophilaMe31B protein, DrosophilamRNA decapping enzymesPatr-1 protein, DrosophilaRecombinant Fusion ProteinsRibonucleasesRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA CapsRNA, MessengerTranscription Factors

Identifiers

PMID20404111
PMCPMC2856893

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.