Evidence map›Paper›PMID 25429105›Full record

ArticleThe Journal of biological chemistry2015

Regulation of ceramide synthase by casein kinase 2-dependent phosphorylation in Saccharomyces cerevisiae.

Tara Fresques, Brad Niles, Sofia Aronova, Huzefa Mogri, Taha Rakhshandehroo, Ted Powers

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

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  5. Structure of the yeast ceramide synthase.Nature structural & molecular biology · 2025
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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

6 authors at 1 institution in 1 country.

Tara FresquesFrom the Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, California 95616.
Brad NilesFrom the Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, California 95616.
Sofia AronovaFrom the Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, California 95616.
Huzefa MogriFrom the Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, California 95616.
Taha RakhshandehrooFrom the Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, California 95616.
Ted PowersFrom the Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, California 95616 tpowers@ucdavis.edu.
University of California, Davis · US

Funding

TOR Complex 2 and sphingolipid biosynthesis.R01GM086387 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI POWERS, TED · 2009 to 2012
$1.3M
NIGMS NIH HHS GM086387NIGMS NIH HHS R01 GM086387
6 · The paper itself

Abstract

Complex sphingolipids are important components of eukaryotic cell membranes and, together with their biosynthetic precursors, including sphingoid long chain bases and ceramides, have important signaling functions crucial for cell growth and survival. Ceramides are produced at the endoplasmic reticulum (ER) membrane by a multicomponent enzyme complex termed ceramide synthase (CerS). In budding yeast, this complex is composed of two catalytic subunits, Lac1 and Lag1, as well as an essential regulatory subunit, Lip1. Proper formation of ceramides by CerS has been shown previously to require the Cka2 subunit of casein kinase 2 (CK2), a ubiquitous enzyme with multiple cellular functions, but the precise mechanism involved has remained unidentified. Here we present evidence that Lac1 and Lag1 are direct targets for CK2 and that phosphorylation at conserved positions within the C-terminal cytoplasmic domain of each protein is required for optimal CerS activity. Our data suggest that phosphorylation of Lac1 and Lag1 is important for proper localization and distribution of CerS within the ER membrane and that phosphorylation of these sites is functionally linked to the COP I-dependent C-terminal dilysine ER retrieval pathway. Together, our data identify CK2 as an important regulator of sphingolipid metabolism, and additionally, because both ceramides and CK2 have been implicated in the regulation of cancer, our findings may lead to an enhanced understanding of their relationship in health and disease.

Indexed as

Gene Expression Regulation, FungalAmino Acid MotifsAmino Acid SequenceCasein Kinase IICatalytic DomainCeramidesEndoplasmic ReticulumHumansMembrane ProteinsMicroscopy, FluorescenceMolecular Sequence DataOxidoreductasesPhosphorylationPlasmidsRecombinant ProteinsSaccharomyces cerevisiaeCasein Kinase IICeramidesdihydroceramide desaturaseLAC1 protein, S cerevisiaeLAG1 protein, S cerevisiaeMembrane ProteinsOxidoreductasesRecombinant ProteinsSaccharomyces cerevisiae ProteinsSphingolipidsEndoplasmic Reticulum (ER)LipidMembraneProtein KinaseSignalingSphingolipidsYeast

Identifiers

PMID25429105
PMCPMC4340386
OpenAlexW2070199965

What OpenQuestion holds

Textmetadata
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.