Evidence map›Paper›PMID 41806112›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2026

ORMDL Proteins Turnover via Proteasome and Autophagy Is Cell-Type Dependent and Tied to Ceramide Homeostasis.

Michal Mrkacek, Magda Tumova, Alex Puskasu, Pavol Utekal, Marek Vrbacky, Ladislav Kuchar, Petr Draber, Viktor Bugajev

Abstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Michal MrkacekLaboratory of Signal Transduction, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic.ORCID https://orcid.org/0009-0004-6478-1894
Magda TumovaLaboratory of Signal Transduction, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic.ORCID https://orcid.org/0000-0002-2636-1707
Alex PuskasuLaboratory of Signal Transduction, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic.ORCID https://orcid.org/0009-0002-2955-0180
Pavol UtekalLaboratory of Signal Transduction, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic.ORCID https://orcid.org/0009-0007-0596-246X
Marek VrbackyLaboratory of Bioenergetics, Institute of Physiology of the Czech Academy of Sciences, Prague, Czech Republic.ORCID https://orcid.org/0000-0001-7218-8370
Ladislav KucharResearch Unit for Rare Diseases, Department of Pediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University and General University Hospital in Prague, Prague, Czech Republic.ORCID https://orcid.org/0000-0003-0721-6624
Petr DraberLaboratory of Signal Transduction, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic.ORCID https://orcid.org/0000-0002-3986-2025
Viktor BugajevLaboratory of Signal Transduction, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic.ORCID https://orcid.org/0000-0003-1262-4438

Funding

Grantová Agentura České Republiky (GAČR) 23-07736SGrantová Agentura České Republiky (GAČR) 24-12572SMinisterstvo Školství, Mládeže a Tělovýchovy (MŠMT) ID CZ.02.01.01/00/23_020/0008540Ministerstvo Školství, Mládeže a Tělovýchovy (MŠMT) ID LX22NPO5102Ministerstvo Zdravotnictví Ceské Republiky (MZCR) NU21-08-00324ÚMG | Czech Centre for Phenogenomics, Institute of Molecular Genetics of the Czech Academy of Sciences (CCP) RVO 68378050Univerzita Karlova v Praze (UK) UNCE/MED/007
6 · The paper itself

Abstract

ORMDL proteins are essential negative regulators of the serine palmitoyltransferase (SPT) complex, thereby controlling the rate of de novo sphingolipid synthesis. Although mammalian ORMDLs undergo rapid turnover, the mechanisms regulating their stability remain unclear, with conflicting observations across studies. Here, we combined lipidomics, proteomics, and biochemical assays to investigate ORMDL regulation in HEK293, RPE-1, and primary mouse bone marrow-derived mast cells (BMMCs). Inhibition of SPT by myriocin or of ceramide synthases by fumonisin B

Indexed as

AutophagyCeramidesHomeostasisMembrane ProteinsProteasome Endopeptidase ComplexAnimalsFatty Acids, MonounsaturatedFumonisinsHEK293 CellsHumansMiceSerine C-PalmitoyltransferaseSphingolipidsCeramidesFatty Acids, Monounsaturatedfumonisin B1FumonisinsMembrane ProteinsORMDL3 protein, mouseProteasome Endopeptidase ComplexSerine C-PalmitoyltransferaseSphingolipidsthermozymocidinautophagyfumonisin B1LC3myriocinORMDL3proteasome degradationRRIDsphingolipid

Identifiers

PMID41806112
PMCPMC12974560

What OpenQuestion holds

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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.