Evidence map›Paper›PMID 30936184›Full record

ArticleJournal of lipid research2019

The triglyceride synthesis enzymes DGAT1 and DGAT2 have distinct and overlapping functions in adipocytes.

Chandramohan Chitraju, Tobias C Walther, Robert V Farese

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
14.0field-weighted citation impact, top 1% 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

104 citing papers in PubMed, 200 citations in OpenAlex.

  1. Local Suppression ofJournal of microbiology and biotechnology · 2026
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  9. An Aqueous Extract ofInternational journal of molecular sciences · 2026
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44 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Chandramohan ChitrajuDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA 02115.
Tobias C WaltherDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA 02115 twalther@hsph.harvard.edu robert@hsph.harvard.edu.
Robert V FareseDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA 02115 twalther@hsph.harvard.edu robert@hsph.harvard.edu.
Harvard University · USBroad Institute · US

Funding

ROLE OF DGAT IN TRIACYLGLYCEROL METABOLISMR01DK056084 · NIDDK · J. DAVID GLADSTONE INSTITUTES · PI FARESE, ROBERT V · 2000 to 2014
$6.4M
Mechanisms of Lipid Droplet Protein TargetingR01GM097194 · NIGMS · YALE UNIVERSITY · PI WALTHER, TOBIAS C · 2011 to 2024
$4.9M
Mechanisms of Lipid Droplet FormationR01GM124348 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI FARESE, ROBERT V · 2017 to 2024
$2.9M
Physiology of Lipid Droplets and Triglyceride StorageR01DK101579 · NIDDK · HARVARD SCHOOL OF PUBLIC HEALTH · PI FARESE, ROBERT V · 2014 to 2018
$2.6M
Howard Hughes Medical InstituteNIDDK NIH HHS R01 DK056084NIDDK NIH HHS R01 DK101579NIGMS NIH HHS R01 GM097194NIGMS NIH HHS R01 GM124348
6 · The paper itself

Abstract

Mammals store metabolic energy as triacylglycerols (TGs) in adipose tissue. TG synthesis is catalyzed by the evolutionarily unrelated acyl-CoA:diacylglycerol acyltransferase (DGAT) enzymes DGAT1 and DGAT2, which catalyze the same reaction and account for nearly all TG synthesis. The reasons for their convergent evolution to synthesize TGs remain unclear. Mice lacking DGAT1 are viable with reduced fat stores of TGs, whereas DGAT2 KO mice die postnatally just after birth with >90% reduction of TGs, suggesting that DGAT2 is the predominant enzyme for TG storage. To better understand the functional differences between the DGATs, we studied mice fed chow or high-fat diets lacking either enzyme in adipose tissue. Unexpectedly, mice lacking DGAT2 in adipocytes have normal TG storage and glucose metabolism on regular or high-fat diets, indicating DGAT2 is not essential for fat storage. In contrast, mice lacking DGAT1 in adipocytes have normal TG storage on a chow diet but moderately decreased body fat accompanied by glucose intolerance when challenged with a high-fat diet. The latter changes were associated with the activation of ER stress pathways. We conclude that DGAT1 and DGAT2 can largely compensate for each other for TG storage but that DGAT1 uniquely has an important role in protecting the ER from the lipotoxic effects of high-fat diets.

Indexed as

AdipocytesAdipose TissueAnimalsDiacylglycerol O-AcyltransferaseDiet, High-FatEndoplasmic Reticulum StressEpidermisImmunoblottingMiceMice, Inbred C57BLObesityTriglyceridesDgat1 protein, mouseDGAT2 protein, mouseDiacylglycerol O-AcyltransferaseTriglyceridesadipose tissuediacylglycerol acyltransferaseendoplasmic reticulum stressglucose intolerancehigh-fat dietinduced obesity

Identifiers

PMID30936184
PMCPMC6547635
OpenAlexW2932544732

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.