Evidence map›Paper›PMID 37700444›Full record

ArticleGenes to cells : devoted to molecular & cellular mechanisms2023

Yeast Tor complex 1 phosphorylates eIF4E-binding protein, Caf20.

Yoshiaki Kamada, Ryoko Ando, Shingo Izawa, Akira Matsuura

Open access · hybridAbstract read
In one paragraph

Article in Genes to cells : devoted to molecular & cellular mechanisms, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Yeast Tor complex 1 phosphorylates eIF4E-binding protein, Caf20.Genes to cells : devoted to molecular & cellular mechanisms · 2023
    Article
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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

4 authors at 3 institutions in 1 country.

Yoshiaki KamadaNational Institute for Basic Biology, Okazaki, Japan.ORCID https://orcid.org/0000-0001-7395-660X
Ryoko AndoDepartment of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Kyoto, Japan.
Shingo IzawaDepartment of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Kyoto, Japan.
Akira MatsuuraDepartment of Biology, Graduate School of Science, Chiba University, Chiba, Japan.ORCID https://orcid.org/0000-0002-2300-7227
Kyoto Institute of Technology · JPChiba University · JPNational Institute for Basic Biology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tor complex 1 (TORC1), a master regulator of cell growth, is an evolutionarily conserved protein kinase within eukaryotic organisms. To control cell growth, TORC1 governs translational processes by phosphorylating its substrate proteins in response to cellular nutritional cues. Mammalian TORC1 (mTORC1) assumes the responsibility of phosphorylating the eukaryotic translation initiation factor 4E (eIF4E)-binding protein 1 (4E-BP1) to regulate its interaction with eIF4E. The budding yeast Saccharomyces cerevisiae possesses a pair of 4E-BP genes, CAF20 and EAP1. However, the extent to which the TORC1-4E-BP axis regulates translational initiation in yeast remains uncertain. In this study, we demonstrated the influence of TORC1 on the phosphorylation status of Caf20 in vivo, as well as the direct phosphorylation of Caf20 by TORC1 in vitro. Furthermore, we found the TORC1-dependent recruitment of Caf20 to the 80S ribosome. Consequently, our study proposes a plausible involvement of yeast's 4E-BP in the efficacy of translation initiation, an aspect under the control of TORC1.

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAnimalsCell Cycle ProteinsMammalsMechanistic Target of Rapamycin Complex 1Peptide Initiation FactorsPhosphoproteinsPhosphorylationProtein BindingProtein BiosynthesisTranscription FactorsCaf20 protein, S cerevisiaeCell Cycle ProteinsMechanistic Target of Rapamycin Complex 1Peptide Initiation FactorsPhosphoproteinsSaccharomyces cerevisiae ProteinsTranscription Factors4E-BPsignal transductionTorTORC1translation initiationyeast

Identifiers

PMID37700444
PMCPMC11447835
OpenAlexW4386703771

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.