Evidence map›Paper›PMID 29278326›Full record

ArticleBiochemistry2018

Functional Contribution of the Spastic Paraplegia-Related Triglyceride Hydrolase DDHD2 to the Formation and Content of Lipid Droplets.

Jordon M Inloes, William B Kiosses, Huajin Wang, Tobias C Walther, Robert V Farese, Benjamin F Cravatt

Abstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.5field-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

40 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Review
  3. DDHD2 possesses both lipase and transacylase capacities that remodel triglyceride acyl chains.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Microglia-to-neuron signaling linksProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Review
  9. Ceramide homeostasis in hepatic lipid droplets.Biochemical Society transactions · 2025
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Functions of Stress-Induced Lipid Droplets in the Nervous System.Frontiers in cell and developmental biology · 2022
    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

6 authors at 3 institutions in 1 country.

Jordon M InloesDepartment of Chemical Physiology, The Skaggs Institute for Chemical Biology, The Scripps Research Institute , La Jolla, California 92037, United States.
William B KiossesDepartment of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute , La Jolla, California 92037, United States.
Huajin WangUniversity Libraries, Carnegie Mellon University , Pittsburgh, Pennsylvania 15213, United States.
Tobias C WaltherDepartment of Genetics and Complex Diseases, Harvard T. H. Chan School of Public Health , Boston, Massachusetts 02115, United States.
Robert V FareseDepartment of Genetics and Complex Diseases, Harvard T. H. Chan School of Public Health , Boston, Massachusetts 02115, United States.
Benjamin F CravattDepartment of Chemical Physiology, The Skaggs Institute for Chemical Biology, The Scripps Research Institute , La Jolla, California 92037, United States.ORCID 0000-0001-5330-3492
Scripps Research Institute · USBroad Institute · USHarvard University · US

Funding

CHEMOPROTEOMIC METHODS FOR SERINE HYDROLASE INHIBITOR DEVELOPMENTR01DA033760 · NIDA · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F, SCAMPAVIA, LOUIS DANIEL · 2012 to 2021
$5.1M
Mechanisms of Lipid Droplet Protein TargetingR01GM097194 · NIGMS · YALE UNIVERSITY · PI WALTHER, TOBIAS C · 2011 to 2024
$4.9M
NIDA NIH HHS R01 DA033760NIGMS NIH HHS R01 GM097194
6 · The paper itself

Abstract

Deleterious mutations in the serine lipase DDHD2 are a causative basis of complex hereditary spastic paraplegia (HSP, subtype SPG54) in humans. We recently found that DDHD2 is a principal triglyceride hydrolase in the central nervous system (CNS) and that genetic deletion of this enzyme in mice leads to ectopic lipid droplet (LD) accumulation in neurons throughout the brain. Nonetheless, how HSP-related mutations in DDHD2 relate to triglyceride metabolism and LD formation remains poorly understood. Here, we have characterized a set of HSP-related mutations in DDHD2 and found that they disrupt triglyceride hydrolase activity in vitro and impair the capacity of DDHD2 to protect cells from LD accumulation following exposure to free fatty acid, an outcome that was also observed with a DDHD2-selective inhibitor. We furthermore isolated and characterized LDs from brain tissue of DDHD2

Indexed as

AnimalsBrain ChemistryCatalytic DomainFatty AcidsHomeostasisHumansLipid Droplet Associated ProteinsLipid DropletsMiceMice, KnockoutMicroscopy, ConfocalMutagenesis, Site-DirectedNerve Tissue ProteinsOrgan SpecificityPhospholipasesPhospholipases A1DDHD2 protein, humanDDHD2 protein, mouseFatty AcidsLipid Droplet Associated ProteinsNerve Tissue ProteinsPhospholipasesPhospholipases A1Recombinant ProteinsTriglycerides

Identifiers

PMID29278326
PMCPMC5854151
OpenAlexW2777032173

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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.