ArticlePlant physiology2026
Opposite diacylglycerol enantiomeric specificities of Arabidopsis DGAT1 and DGAT2 reveal distinct roles in TAG synthesis.
Article in Plant physiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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.
Who cites it
1 citing paper in PubMed.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Triacylglycerol (TAG) serves as the primary storage lipid in plants, essential for seed germination and early seedling development. Acyl-CoA:diacylglycerol acyltransferase (DGAT) enzymes catalyze the last step in TAG synthesis by converting diacylglycerol (DAG) to TAG. Although functionally conserved across species, DGATs exhibit variations in substrate preference, among their other properties, highlighting their influence on fatty acid (FA) composition in TAG. In this study, we investigated the biochemical properties of Arabidopsis DGATs expressed in yeast with a primary emphasis on understanding the specificity and selectivity of these enzymes on different acyl acceptors and donors. One aim of the study was to investigate if the FA composition of TAG is due to DGAT selectivity in addition to being influenced by the distinct DAG pools (spatially separated de novo synthesized and phosphatidylcholine [PC]-derived DAG). Our findings showed that Arabidopsis (Arabidopsis thaliana) DGAT1 preferentially selects PC-derived DAGs. Further, we also report a new method for synthesizing sn-2,3-DAG that we used to study DGAT enantiomeric specificity. The results revealed that DGAT1 is specific toward the sn-1,2-DAG enantiomer whereas DGAT2 only utilizes sn-2,3-DAG, a substrate that is not directly involved in the Kennedy pathway. DGAT2 has so far not shown significant involvement in de novo TAG synthesis and thus our findings indicate a possible function for DGAT2 in Arabidopsis in TAG remodeling.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.