Evidence map›Paper›PMID 29927351›Full record

ArticleMolecular biology of the cell2018

TOR complex 2-regulated protein kinase Ypk1 controls sterol distribution by inhibiting StARkin domain-containing proteins located at plasma membrane-endoplasmic reticulum contact sites.

Françoise M Roelants, Neha Chauhan, Alexander Muir, Jameson C Davis, Anant K Menon, Timothy P Levine, Jeremy Thorner

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  4. bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Review of methods for the determination of cellular cholesterol content: principles, advantages, limitations, applications, and perspectives.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Review
  7. Article
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Review
  14. The functional universe of membrane contact sites.Nature reviews. Molecular cell biology · 2020
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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

7 authors at 3 institutions in 2 countries.

Françoise M RoelantsDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720-3202.
Neha ChauhanDepartment of Biochemistry, Weill Cornell Medical College, New York, NY 10065.
Alexander MuirDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720-3202.
Jameson C DavisDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720-3202.
Anant K MenonDepartment of Biochemistry, Weill Cornell Medical College, New York, NY 10065.
Timothy P LevineUCL Institute of Ophthalmology, University College London, London EC1V 9EL, UK.
Jeremy ThornerDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720-3202.
University of California, Berkeley · USCornell University · USUniversity College London · GB

Funding

Yeast Protein Kinase Signaling Networks: Specificity, Regulation and FunctionR01GM021841 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THORNER, JEREMY W. · 1985 to 2019
$11.8M
Biotechnology and Biological Sciences Research Council BB/P003818Biotechnology and Biological Sciences Research Council BB/P003818/1NIGMS NIH HHS R01 GM021841
6 · The paper itself

Abstract

In our proteome-wide screen, Ysp2 (also known as Lam2/Ltc4) was identified as a likely physiologically relevant target of the TOR complex 2 (TORC2)-dependent protein kinase Ypk1 in the yeast Saccharomyces cerevisiae. Ysp2 was subsequently shown to be one of a new family of sterol-binding proteins located at plasma membrane (PM)-endoplasmic reticulum (ER) contact sites. Here we document that Ysp2 and its paralogue Lam4/Ltc3 are authentic Ypk1 substrates in vivo and show using genetic and biochemical criteria that Ypk1-mediated phosphorylation inhibits the ability of these proteins to promote retrograde transport of sterols from the PM to the ER. Furthermore, we provide evidence that a change in PM sterol homeostasis promotes cell survival under membrane-perturbing conditions known to activate TORC2-Ypk1 signaling. These observations define the underlying molecular basis of a new regulatory mechanism for cellular response to plasma membrane stress.

Indexed as

Cell MembraneEndoplasmic ReticulumHomeostasisMechanistic Target of Rapamycin Complex 2PhosphorylationProtein DomainsProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSphingolipidsSterolsStress, PhysiologicalMechanistic Target of Rapamycin Complex 2Protein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSphingolipidsSterolsYPK1 protein, S cerevisiae

Identifiers

PMID29927351
PMCPMC6232965
OpenAlexW2809449425

What OpenQuestion holds

Textmetadata
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.