Evidence map›Paper›PMID 35758748›Full record

ArticleMicrobiology spectrum2022

Microdomain Protein Nce102 Is a Local Sensor of Plasma Membrane Sphingolipid Balance.

Jakub Zahumenský, Caroline Mota Fernandes, Petra Veselá, Maurizio Del Poeta, James B Konopka, Jan Malínský

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2022. 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
2.0field-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

11 citing papers in PubMed, 18 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

6 authors at 3 institutions in 2 countries.

Jakub ZahumenskýDepartment of Functional Organization of Biomembranes, Institute of Experimental Medicine, Academy of Sciences of the Czech Republic, Prague, Czech Republic.ORCID 0000-0002-8332-9789
Caroline Mota FernandesDepartment of Microbiology and Immunology, School of Medicine, Stony Brook Universitygrid.36425.36, Stony Brook, New York, USA.
Petra VeseláDepartment of Functional Organization of Biomembranes, Institute of Experimental Medicine, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
Maurizio Del PoetaDepartment of Microbiology and Immunology, School of Medicine, Stony Brook Universitygrid.36425.36, Stony Brook, New York, USA.ORCID 0000-0001-8418-3120
James B KonopkaDepartment of Microbiology and Immunology, School of Medicine, Stony Brook Universitygrid.36425.36, Stony Brook, New York, USA.ORCID 0000-0001-5989-4086
Jan MalínskýDepartment of Functional Organization of Biomembranes, Institute of Experimental Medicine, Academy of Sciences of the Czech Republic, Prague, Czech Republic.ORCID 0000-0002-1433-0989
Czech Academy of Sciences, Institute of Experimental Medicine · CZStony Brook University · USNorthport VA Medical Center · US

Funding

Regulation of Morphogenesis in C. albicansR01AI047837 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI James B Konopka · 2001 to 2026
$8.8M
New antifungals targeting the synthesis of fungal sphingolipidsR01AI116420 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI Maurizio Del Poeta · 2016 to 2026
$7.6M
Lipid-mediated fungal pathogenesisR01AI125770 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI DEL POETA, MAURIZIO · 2016 to 2025
$6.2M
Role of host spingolipids against fungal infectionsI01BX002624 · VA · NORTHPORT VA MEDICAL CENTER · PI Maurizio Del Poeta · 2016 to 2026
–
BLRD Research Career Scientist Award ApplicationIK6BX005386 · VA · NORTHPORT VA MEDICAL CENTER · PI DEL POETA, MAURIZIO · 2021 to 2025
–
BLRD VA I01 BX002624BLRD VA IK6 BX005386NIAID NIH HHS R01 AI047837NIAID NIH HHS R01 AI116420NIAID NIH HHS R01 AI125770
6 · The paper itself

Abstract

Sphingolipids are essential building blocks of eukaryotic membranes and important signaling molecules that are regulated tightly in response to environmental and physiological inputs. While their biosynthetic pathway has been well-described, the mechanisms that facilitate the perception of sphingolipid levels at the plasma membrane remain to be uncovered. In Saccharomyces cerevisiae, the Nce102 protein has been proposed to function as a sphingolipid sensor as it changes its plasma membrane distribution in response to sphingolipid biosynthesis inhibition. We show that Nce102 redistributes specifically in regions of increased sphingolipid demand, e.g., membranes of nascent buds. Furthermore, we report that the production of Nce102 increases following sphingolipid biosynthesis inhibition and that Nce102 is internalized when excess sphingolipid precursors are supplied. This finding suggests that the total amount of Nce102 in the plasma membrane is a measure of the current need for sphingolipids, whereas its local distribution marks sites of high sphingolipid demand. The physiological role of Nce102 in the regulation of sphingolipid synthesis is demonstrated by mass spectrometry analysis showing reduced levels of hydroxylated complex sphingolipids in response to heat stress in the

Indexed as

Saccharomyces cerevisiae ProteinsSphingolipidsCandida albicansCell MembraneFungal ProteinsSaccharomyces cerevisiaeFungal ProteinsNCE102 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSphingolipidseisosomemicrodomainplasma membranesphingolipidstress sensor

Identifiers

PMID35758748
PMCPMC9431316
OpenAlexW4283580414

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.