Evidence map›Paper›PMID 36149412›Full record

ArticleThe Biochemical journal2022

TOR complex 2 is a master regulator of plasma membrane homeostasis.

Jeremy Thorner

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Functional analysis of target of rapamycin in regulating mycelial growth and development in Penicillium italicum.International microbiology : the official journal of the Spanish Society for Microbiology · 2026
    Article
  4. Article
  5. Article
  6. bioRxiv : the preprint server for biology · 2025
    Article
  7. NADCells · 2025
    Review
  8. Article
  9. Article
  10. Making PI3K superfamily enzymes run faster.Advances in biological regulation · 2025
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. TOR Complex 1: Orchestrating Nutrient Signaling and Cell Cycle Progression.International journal of molecular sciences · 2023
    Review
  17. Article
  18. Review
  19. Article
  20. 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

1 author at 1 institution in 1 country.

Jeremy ThornerDivision of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, U.S.A.ORCID 0000-0002-2583-500X
University of California, Berkeley · US

Funding

Yeast Protein Kinase Signaling Networks: Specificity, Regulation and FunctionR01GM021841 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THORNER, JEREMY W. · 1985 to 2019
$11.8M
NIGMS NIH HHS R01 GM021841
6 · The paper itself

Abstract

As first demonstrated in budding yeast (Saccharomyces cerevisiae), all eukaryotic cells contain two, distinct multi-component protein kinase complexes that each harbor the TOR (Target Of Rapamycin) polypeptide as the catalytic subunit. These ensembles, dubbed TORC1 and TORC2, function as universal, centrally important sensors, integrators, and controllers of eukaryotic cell growth and homeostasis. TORC1, activated on the cytosolic surface of the lysosome (or, in yeast, on the cytosolic surface of the vacuole), has emerged as a primary nutrient sensor that promotes cellular biosynthesis and suppresses autophagy. TORC2, located primarily at the plasma membrane, plays a major role in maintaining the proper levels and bilayer distribution of all plasma membrane components (sphingolipids, glycerophospholipids, sterols, and integral membrane proteins). This article surveys what we have learned about signaling via the TORC2 complex, largely through studies conducted in S. cerevisiae. In this yeast, conditions that challenge plasma membrane integrity can, depending on the nature of the stress, stimulate or inhibit TORC2, resulting in, respectively, up-regulation or down-regulation of the phosphorylation and thus the activity of its essential downstream effector the AGC family protein kinase Ypk1. Through the ensuing effect on the efficiency with which Ypk1 phosphorylates multiple substrates that control diverse processes, membrane homeostasis is maintained. Thus, the major focus here is on TORC2, Ypk1, and the multifarious targets of Ypk1 and how the functions of these substrates are regulated by their Ypk1-mediated phosphorylation, with emphasis on recent advances in our understanding of these processes.

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell MembraneGlycerophospholipidsHomeostasisMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2Membrane ProteinsProtein KinasesSphingolipidsSterolsGlycerophospholipidsMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2Membrane ProteinsProtein KinasesSaccharomyces cerevisiae ProteinsSphingolipidsSterolscontact siteslipidsmembrane proteinsphosphorylationplasma membraneprotein kinases

Identifiers

PMID36149412
PMCPMC9555796
OpenAlexW4296794156

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.