Evidence map›Paper›PMID 25117580›Full record

ArticlePloS one2014

TORC1 regulates Pah1 phosphatidate phosphatase activity via the Nem1/Spo7 protein phosphatase complex.

Emmanuelle Dubots, Stéphanie Cottier, Marie-Pierre Péli-Gulli, Malika Jaquenoud, Séverine Bontron, Roger Schneiter, Claudio De Virgilio

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

37 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  11. A Yeast Mitotic Tale for the Nucleus and the Vacuoles to Embrace.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Autophagy of the Nucleus in Health and Disease.Frontiers in cell and developmental biology · 2021
    Review
  19. Article
  20. Nucleophagy-Implications for Microautophagy and Health.International journal of molecular sciences · 2020
    Review
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 at 1 institution in 1 country.

Emmanuelle DubotsDepartment of Biology, University of Fribourg, CH-1700 Fribourg, Switzerland.
Stéphanie CottierDepartment of Biology, University of Fribourg, CH-1700 Fribourg, Switzerland.
Marie-Pierre Péli-GulliDepartment of Biology, University of Fribourg, CH-1700 Fribourg, Switzerland.
Malika JaquenoudDepartment of Biology, University of Fribourg, CH-1700 Fribourg, Switzerland.
Séverine BontronDepartment of Biology, University of Fribourg, CH-1700 Fribourg, Switzerland.
Roger SchneiterDepartment of Biology, University of Fribourg, CH-1700 Fribourg, Switzerland.
Claudio De VirgilioDepartment of Biology, University of Fribourg, CH-1700 Fribourg, Switzerland.
University of Fribourg · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The evolutionarily conserved target of rapamycin complex 1 (TORC1) controls growth-related processes such as protein, nucleotide, and lipid metabolism in response to growth hormones, energy/ATP levels, and amino acids. Its deregulation is associated with cancer, type 2 diabetes, and obesity. Among other substrates, mammalian TORC1 directly phosphorylates and inhibits the phosphatidate phosphatase lipin-1, a central enzyme in lipid metabolism that provides diacylglycerol for the synthesis of membrane phospholipids and/or triacylglycerol as neutral lipid reserve. Here, we show that yeast TORC1 inhibits the function of the respective lipin, Pah1, to prevent the accumulation of triacylglycerol. Surprisingly, TORC1 regulates Pah1 in part indirectly by controlling the phosphorylation status of Nem1 within the Pah1-activating, heterodimeric Nem1-Spo7 protein phosphatase module. Our results delineate a hitherto unknown TORC1 effector branch that controls lipin function in yeast, which, given the recent discovery of Nem1-Spo7 orthologous proteins in humans, may be conserved.

Indexed as

Enzyme ActivationFungal ProteinsHumansMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesNuclear ProteinsPhosphatidate PhosphatasePhosphorylationProtein BindingTOR Serine-Threonine KinasesFungal ProteinsLPIN1 protein, humanMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesNuclear ProteinsPhosphatidate PhosphataseTOR Serine-Threonine Kinases

Identifiers

PMID25117580
PMCPMC4130541
OpenAlexW2059643803

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.