Evidence map›Paper›PMID 34445723›Full record

ArticleInternational journal of molecular sciences2021

Target of Rapamycin Complex 1 (TORC1), Protein Kinase A (PKA) and Cytosolic pH Regulate a Transcriptional Circuit for Lipid Droplet Formation.

Vitor Teixeira, Telma S Martins, William A Prinz, Vítor Costa

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

8 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The Plasma Membrane HInternational journal of molecular sciences · 2023
    Article
  5. Article
  6. Special Issue: Yeast Cell Signaling Pathways (Volume 1).International journal of molecular sciences · 2023
    Article
  7. Review
  8. 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

4 authors at 2 institutions in 2 countries.

Vitor TeixeiraYeast Signalling Networks, i3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, 4200-135 Porto, Portugal.ORCID 0000-0002-2179-2946
Telma S MartinsYeast Signalling Networks, i3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, 4200-135 Porto, Portugal.
William A PrinzLaboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, MD 20892, USA.
Vítor CostaYeast Signalling Networks, i3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, 4200-135 Porto, Portugal.ORCID 0000-0002-7868-4663
Universidade do Porto · PTNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Intracellular Lipid Trafficking and Organelle BiogenesisZIADK060004 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI PRINZ, WILLIAM · 2009 to 2022
$8.5M
Biogenesis of the endoplasmic reticulumZIADK060105 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI PRINZ, WILLIAM · 2009 to 2022
$8.5M
Fundação para a Ciência e a Tecnologia CEECIND/00724/2017Fundação para a Ciência e a Tecnologia CEECIND/00724/2017/CP1386/CT0006Fundação para a Ciência e a Tecnologia SFRH/BD/136996/2018Fundação para a Ciência e a Tecnologia UIDB/04293/2020NIDDK NIH HHS Intramural Research Program of The National Institute of Diabetes and Digestive and Kidney Diseases
6 · The paper itself

Abstract

Lipid droplets (LDs) are ubiquitous organelles that fulfill essential roles in response to metabolic cues. The identification of several neutral lipid synthesizing and regulatory protein complexes have propelled significant advance on the mechanisms of LD biogenesis in the endoplasmic reticulum (ER). However, our understanding of signaling networks, especially transcriptional mechanisms, regulating membrane biogenesis is very limited. Here, we show that the nutrient-sensing Target of Rapamycin Complex 1 (TORC1) regulates LD formation at a transcriptional level, by targeting

Indexed as

Cyclic AMP-Dependent Protein KinasesCytosolEndoplasmic ReticulumHydrogen-Ion ConcentrationLipid DropletsLipid MetabolismMechanistic Target of Rapamycin Complex 1Membrane ProteinsProtein Phosphatase 2Repressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTranscription FactorsCyclic AMP-Dependent Protein KinasesMechanistic Target of Rapamycin Complex 1Membrane ProteinsOPI1 protein, S cerevisiaeProtein Phosphatase 2Repressor ProteinsSaccharomyces cerevisiae ProteinsSIT4 protein, S cerevisiaeTORC1 protein complex, S cerevisiaeTranscription Factorscell signalinglipid dropletmembrane biogenesisnutrienttranscription

Identifiers

PMID34445723
PMCPMC8396576
OpenAlexW3194765884

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.