Evidence map›Paper›PMID 16201964›Full record

ArticleThe Biochemical journal2006

Distinct roles for de novo versus hydrolytic pathways of sphingolipid biosynthesis in Saccharomyces cerevisiae.

L Ashley Cowart, Yasuo Okamoto, Xinghua Lu, Yusuf A Hannun

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

L Ashley CowartDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.
Yasuo Okamoto
Xinghua Lu
Yusuf A Hannun
Medical University of South Carolina · US

Funding

UBIQUITIN CARBOXYL TERMINAL HYDROLASE L1 (UCH-L1) AND VASCULAR LESION FORMATIONP20RR016434 · NCRR · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI MARKWALD, ROGER R · 2001 to 2011
$24.8M
Sphingomyelin Turnover and Cellular RegulationR37GM043825 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI HANNUN, YUSUF AWNI · 2007 to 2015
$3.7M
SPHINGOMYELIN TURNOVER AND CELLULAR REGULATIONR01GM043825 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI HANNUN, YUSUF AWNI · 1991 to 2006
$2.2M
Statistical methods for integromics discoveriesR01LM010144 · NLM · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI LU, XINGHUA · 2009 to 2013
$1.6M
Cancer Center Microarray Bioinformatics FacilityR24CA095841 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI ARGRAVES, WILLIAM SCOTT · 2002 to 2006
$1.2M
Sphingolipid-dependent Transcriptional Responses to HeatF32GM068270 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI COWART, LAUREN ASHLEY · 2004 to 2004
$47k
NCI NIH HHS R24 CA095841NCI NIH HHS R24CA095841NCRR NIH HHS P20 RR016434NCRR NIH HHS P20RR016434NIGMS NIH HHS F32 GM068270NIGMS NIH HHS GM068270-01NIGMS NIH HHS GM 43825NIGMS NIH HHS R01 GM043825NIGMS NIH HHS R37 GM043825NLM NIH HHS R01 LM010144
6 · The paper itself

Abstract

Saccharomyces cerevisiae produces the sphingolipid ceramide by de novo synthesis as well as by hydrolysis of complex sphingolipids by Isc1p (inositolphosphoceramide-phospholipase C), which is homologous with the mammalian neutral sphingomyelinases. Though the roles of sphingolipids in yeast stress responses are well characterized, it has been unclear whether Isc1p contributes to stress-induced sphingolipids. The present study was undertaken in order to distinguish the relative roles of de novo sphingolipid biosynthesis versus Isc1p-mediated sphingolipid production in the heat-stress response. Ceramide production was measured at normal and increased temperature in an ISC1 deletion and its parental strain (ISC1 being the gene that codes for Isc1p). The results showed that Isc1p contributes specifically to the formation of the C24-, C24:1- and C26-dihydroceramide species. The interaction between these two pathways of sphingolipid production was confirmed by the finding that ISC1 deletion is synthetically lethal with the lcb1-100 mutation. Interestingly, Isc1p did not contribute significantly to transient cell-cycle arrest or growth at elevated temperature, responses known to be regulated by the de novo pathway. In order to define specific contributions of ISC1, microarray hybridizations were performed, and analyses showed misregulation of genes involved in carbon source utilization and sexual reproduction, which was corroborated by defining a sporulation defect of the isc1Delta strain. These results indicate that the two pathways of ceramide production in yeast interact, but differ in their regulation of ceramides of distinct molecular species and serve distinct cellular functions.

Indexed as

Gene DeletionGene Expression Regulation, FungalHot TemperatureHydrolysisReproductionRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSphingolipidsSpores, FungalType C PhospholipasesISC1 protein, S cerevisiaeRNA, FungalSaccharomyces cerevisiae ProteinsSphingolipidsType C Phospholipases

Identifiers

PMID16201964
PMCPMC1360726
OpenAlexW2094760579

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.