Evidence map›Paper›PMID 22864585›Full record

ArticlePlant physiology2012

A land-plant-specific glycerol-3-phosphate acyltransferase family in Arabidopsis: substrate specificity, sn-2 preference, and evolution.

Weili Yang, Jeffrey P Simpson, Yonghua Li-Beisson, Fred Beisson, Mike Pollard, John B Ohlrogge

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
12.9field-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

105 citing papers in PubMed, 227 citations in OpenAlex.

  1. Article
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  8. Genome-wide analysis of theFrontiers in plant science · 2026
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  10. Genetic mapping and validation of QTL for whitefly resistance in cassava (Manihot esculenta Crantz).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025
    Article
  11. Article
  12. Temperature-dependent polar lignification of a seed coat suberin layer promoting dormancy inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
  14. Review
  15. Review
  16. Genome-Wide Identification of the GPAT Family inPlants (Basel, Switzerland) · 2024
    Article
  17. Article
  18. Article
  19. TheProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article

45 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

6 authors at 1 institution in 1 country.

Weili YangDepartment of Plant Biology, Michigan State University, East Lansing, Michigan 48824, USA.
Jeffrey P Simpson
Yonghua Li-Beisson
Fred Beisson
Mike Pollard
John B Ohlrogge
Michigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arabidopsis (Arabidopsis thaliana) has eight glycerol-3-phosphate acyltransferase (GPAT) genes that are members of a plant-specific family with three distinct clades. Several of these GPATs are required for the synthesis of cutin or suberin. Unlike GPATs with sn-1 regiospecificity involved in membrane or storage lipid synthesis, GPAT4 and -6 are unique bifunctional enzymes with both sn-2 acyltransferase and phosphatase activity resulting in 2-monoacylglycerol products. We present enzymology, pathway organization, and evolutionary analysis of this GPAT family. Within the cutin-associated clade, GPAT8 is demonstrated as a bifunctional sn-2 acyltransferase/phosphatase. GPAT4, -6, and -8 strongly prefer C16:0 and C18:1 ω-oxidized acyl-coenzyme As (CoAs) over unmodified or longer acyl chain substrates. In contrast, suberin-associated GPAT5 can accommodate a broad chain length range of ω-oxidized and unsubstituted acyl-CoAs. These substrate specificities (1) strongly support polyester biosynthetic pathways in which acyl transfer to glycerol occurs after oxidation of the acyl group, (2) implicate GPAT specificities as one major determinant of cutin and suberin composition, and (3) argue against a role of sn-2-GPATs (Enzyme Commission 2.3.1.198) in membrane/storage lipid synthesis. Evidence is presented that GPAT7 is induced by wounding, produces suberin-like monomers when overexpressed, and likely functions in suberin biosynthesis. Within the third clade, we demonstrate that GPAT1 possesses sn-2 acyltransferase but not phosphatase activity and can utilize dicarboxylic acyl-CoA substrates. Thus, sn-2 acyltransferase activity extends to all subbranches of the Arabidopsis GPAT family. Phylogenetic analyses of this family indicate that GPAT4/6/8 arose early in land-plant evolution (bryophytes), whereas the phosphatase-minus GPAT1 to -3 and GPAT5/7 clades diverged later with the appearance of tracheophytes.

Indexed as

Evolution, Molecular1-Acylglycerol-3-Phosphate O-AcyltransferaseAcylationAcyl Coenzyme AArabidopsisArabidopsis ProteinsCell MembraneCloning, MolecularEnzyme ActivationEnzyme AssaysFlowersGlycerolLipidsLysophospholipidsMembrane LipidsMonoglycerides1-Acylglycerol-3-Phosphate O-AcyltransferaseAcyl Coenzyme AArabidopsis ProteinscutinGlycerolGPAT5 protein, ArabidopsisLipidslysophosphatidic acidLysophospholipidsMembrane LipidsMonoglyceridesPhosphoric Monoester HydrolasesRecombinant Proteinssuberin

Identifiers

PMID22864585
PMCPMC3461545
OpenAlexW2171655011

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.