Evidence map›Paper›PMID 39024283›Full record

ArticleMolecular biology of the cell2024

Dysregulation of ceramide metabolism causes phytoceramide-dependent induction of the unfolded protein response.

Tamayanthi Rajakumar, Md Amin Hossain, Sylwia A Stopka, Yagmur Micoogullari, Jessie Ang, Nathalie Y R Agar, John Hanna

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular biology of the cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
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

7 authors.

Tamayanthi RajakumarDepartment of Pathology, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Md Amin HossainDepartment of Neurosurgery, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Sylwia A StopkaDepartment of Neurosurgery, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Yagmur MicoogullariDepartment of Pathology, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Jessie AngDepartment of Pathology, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Nathalie Y R AgarDepartment of Neurosurgery, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
John HannaDepartment of Pathology, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.

Funding

Role of very long chain fatty acids in protein quality control and membrane homeostasisR01GM135337 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI HANNA, JOHN W · 2020 to 2023
$1.6M
NIGMS NIH HHS R01 GM135337
6 · The paper itself

Abstract

The unfolded protein response (UPR) detects and mitigates the harmful effects of dysregulated endoplasmic reticulum (ER) function. The UPR has been best characterized as a protein quality control response, and the sole UPR sensor in yeast, Ire1, is known to detect misfolded ER proteins. However, recent work suggests the UPR can also sense diverse defects within the ER membrane, including increased fatty acid saturation and altered phospholipid abundance. These and other lipid-related stimuli have been referred to as lipid bilayer stress and may be sensed independently through Ire1's transmembrane domain. Here, we show that the loss of Isc1, a phospholipase that catabolizes complex ceramides, causes UPR induction, even in the absence of exogenous stress. A series of chemical and genetic approaches identified a requirement for very long-chain fatty acid (VLCFA)-containing phytoceramides for UPR induction. In parallel, comprehensive lipidomics analyses identified large increases in the abundance of specific VLCFA-containing phytoceramides in the

Indexed as

CeramidesEndoplasmic ReticulumEndoplasmic Reticulum StressSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUnfolded Protein ResponseFatty AcidsPhospholipasesType C PhospholipasesCeramidesFatty AcidsISC1 protein, S cerevisiaePhospholipasesSaccharomyces cerevisiae ProteinsType C Phospholipases

Identifiers

PMID39024283
PMCPMC11449394

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.