Evidence map›Paper›PMID 23737533›Full record

ArticleThe Journal of biological chemistry2013

Orm proteins integrate multiple signals to maintain sphingolipid homeostasis.

Charulatha Gururaj, Ross S Federman, Ross Federman, Amy Chang

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

40 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. ORMDL Proteins Turnover via Proteasome and Autophagy Is Cell-Type Dependent and Tied to Ceramide Homeostasis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Pho85 and PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Article
  16. Article
  17. Article
  18. Comparative Proteomic Analysis ofInternational journal of molecular sciences · 2019
    Article
  19. Article
  20. Review
4 · The record

Corrections and comments

  • Erratum issued
    Federman, Ross [corrected to Federman, Ross S]
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Charulatha GururajDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.
Ross S Federman
Ross Federman
Amy Chang
University of Michigan–Ann Arbor · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sphingolipids are structural components of membranes, and sphingolipid metabolites serve as signaling molecules. The first and rate-limiting step in sphingolipid synthesis is catalyzed by serine palmitoyltransferase (SPT). The recently discovered SPT-associated proteins, Orm1 and Orm2, are critical regulators of sphingolipids. Orm protein phosphorylation mediating feedback regulation of SPT activity occurs in response to multiple sphingolipid intermediates, including long chain base and complex sphingolipids. Both branches of the TOR signaling network, TORC1 and TORC2, participate in regulating sphingolipid synthesis via Orm phosphorylation in response to sphingolipid intermediates as well as nutritional conditions. Moreover, sphingolipid synthesis is regulated in response to endoplasmic reticulum (ER) stress by activation of a calcium- and calcineurin-dependent pathway via transcriptional induction of ORM2. Conversely, the calcium- and calcineurin-dependent pathway signals ER stress response upon lipid dysregulation in the absence of the Orm proteins to restore ER homeostasis.

Indexed as

HomeostasisSignal TransductionAdaptor Proteins, Signal TransducingBlotting, WesternCalcineurinCalciumEndoplasmic ReticulumFeedback, PhysiologicalMechanistic Target of Rapamycin Complex 2Membrane ProteinsModels, BiologicalMultiprotein ComplexesMutationPhosphorylationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingCalcineurinCalciumISC1 protein, S cerevisiaeMechanistic Target of Rapamycin Complex 2Membrane ProteinsMultiprotein ComplexesOrm1 protein, S cerevisiaeOrm2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSerine C-PalmitoyltransferaseSphingolipidsTORC1 protein complex, S cerevisiaeTOR Serine-Threonine KinasesTranscription FactorsTSC3 protein, S cerevisiaeType C PhospholipasesCalcineurinER StressPhosphorylationSignal TransductionSphingolipidTOR

Identifiers

PMID23737533
PMCPMC3711311
OpenAlexW2083049407

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.