Evidence map›Paper›PMID 27402848›Full record

ArticleThe Journal of biological chemistry2016

Misregulation of a DDHD Domain-containing Lipase Causes Mitochondrial Dysfunction in Yeast.

Pradeep Kumar Yadav, Ram Rajasekharan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
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  9. Article
  10. Lipids and Secretory Vesicle Exocytosis.Advances in neurobiology · 2023
    Article
  11. Review
  12. Article
  13. Review
  14. Phospholipid turnover and acyl chain remodeling in the yeast ER.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  15. Article
  16. Review
  17. Article
  18. The role of yeast mCurrent genetics · 2018
    Review
  19. The mCurrent genetics · 2018
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  20. Article
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

2 authors at 1 institution in 1 country.

Pradeep Kumar YadavFrom the Lipidomic Centre, Department of Lipid Science and the Academy of Scientific and Innovative Research, Council of Scientific and Industrial Research (CSIR)-Central Food Technological Research Institute (CFTRI), Mysore 570020, Karnataka, India.
Ram RajasekharanFrom the Lipidomic Centre, Department of Lipid Science and the Academy of Scientific and Innovative Research, Council of Scientific and Industrial Research (CSIR)-Central Food Technological Research Institute (CFTRI), Mysore 570020, Karnataka, India ram@cftri.com.ORCID 0000-0002-2124-6013
Central Food Technological Research Institute · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The DDHD domain-containing proteins, which belong to the intracellular phospholipase A1 (iPLA1) family, have been predicted to be involved in phospholipid metabolism, lipid trafficking, membrane turnover, and signaling. Defective cardiolipin (CL), phosphatidylethanolamine, and phosphatidylglycerol remodeling cause Barth syndrome and mitochondrial dysfunction. Here, we report that Yor022c is a Ddl1 (DDHD domain-containing lipase 1) that hydrolyzes CL, phosphatidylethanolamine, and phosphatidylglycerol. Ddl1 has been implicated in the remodeling of mitochondrial phospholipids and CL degradation. Our data also suggested that the accumulation of monolysocardiolipin is deleterious to the cells. We show that Aft1 and Aft2 transcription factors antagonistically regulate the DDL1 gene. This study reveals that the misregulation of DDL1 by Aft1/2 transcription factors alters CL metabolism and causes mitochondrial dysfunction in the cells. In humans, mutations in the DDHD1 and DDHD2 genes cause specific types of hereditary spastic paraplegia (SPG28 and SPG54, respectively), and the yeast DDL1-defective strain produces similar phenotypes of hereditary spastic paraplegia (mitochondrial dysfunction and defects in lipid metabolism). Therefore, the DDL1-defective strain could be a good model system for understanding hereditary spastic paraplegia.

Indexed as

Gene Expression Regulation, EnzymologicGene Expression Regulation, FungalLipaseMitochondriaMitochondrial ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription FactorsAFT1 protein, S cerevisiaeAft2 protein, S cerevisiaeLipaseMitochondrial ProteinsSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription FactorsAFT1/2 transcription factorsBarth syndromecardiolipinDDHD domaingene regulationhereditary spastic paraplegiametabolismmitochondriaphospholipidYOR022C

Identifiers

PMID27402848
PMCPMC5000100
OpenAlexW2472435867

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.