Evidence map›Paper›PMID 27717283›Full record

ArticleProteomics2016

Proteomic and phosphoproteomic analyses of yeast reveal the global cellular response to sphingolipid depletion.

Florian Fröhlich, Daniel K Olson, Romain Christiano, Robert V Farese, Tobias C Walther

Abstract read
In one paragraph

Article in Proteomics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Structure of the yeast ceramide synthase.Nature structural & molecular biology · 2025
    Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Infection and immunity · 2019
    Article
  8. Article
  9. Review
  10. Article
  11. 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

5 authors at 3 institutions in 2 countries.

Florian FröhlichDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA, USA.
Daniel K OlsonDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA, USA.
Romain ChristianoDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA, USA.
Robert V FareseDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA, USA.
Tobias C WaltherDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA, USA. twalther@hsph.harvard.edu.
Harvard University · USOsnabrück University · DEUniversity of Hawaiʻi at Mānoa · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
Mechanisms of Lipid Droplet Protein TargetingR01GM097194 · NIGMS · YALE UNIVERSITY · PI WALTHER, TOBIAS C · 2011 to 2024
$4.9M
Cellular Functions of Plasma Membrane Organization by EisosomesR01GM095982 · NIGMS · YALE UNIVERSITY · PI WALTHER, TOBIAS C · 2012 to 2015
$1.2M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM095982NIGMS NIH HHS R01 GM097194NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

Sphingolipids are essential components of eukaryotic cells with important functions in membrane biology and cellular signaling. Their levels are tightly controlled and coordinated with the abundance of other membrane lipids. How sphingolipid homeostasis is achieved is not yet well understood. Studies performed primarily in yeast showed that the phosphorylation states of several enzymes and regulators of sphingolipid synthesis are important, although a global understanding for such regulation is lacking. Here, we used high-resolution MS-based proteomics and phosphoproteomics to analyze the cellular response to sphingolipid synthesis inhibition. Our dataset reveals that changes in protein phosphorylation, rather than protein abundance, dominate the response to blocking sphingolipid synthesis. We identified Ypk signaling as a pathway likely to be activated under these conditions, and we identified potential Ypk1 target proteins. Our data provide a rich resource for on-going mechanistic studies of key elements of the cellular response to the depletion of sphingolipid levels and the maintenance of sphingolipid homeostasis. All MS data have been deposited in the ProteomeXchange with identifier PXD003854 (http://proteomecentral.proteomexchange.org/dataset/PXD003854).

Indexed as

ProteomicsHomeostasisPhosphorylationProtein Serine-Threonine KinasesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionSphingolipidsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSphingolipidsYPK1 protein, S cerevisiaeCell biologyMass spectrometryMyriocinPhosphorylationSaccharomyces cerevisiaeSILACSphingolipid metabolism

Identifiers

PMID27717283
PMCPMC5688516
OpenAlexW2526599662

What OpenQuestion holds

Textmetadata
LicenceTDM
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.