Evidence map›Paper›PMID 41337596›Full record

ArticleScience advances2025

Molecular basis of very-long-chain fatty acid elongation by the CER6-GL2 enzyme complex in plant wax biosynthesis.

Yaqi Liu, Yuan Chen, Xue Zhang, Mengxue Li, Ji Wang, Zhao Yang, Miaolian Ma, Zhiwei Zhao, Hongtao Liu, Fang Yu and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Review
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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

11 authors.

Yaqi LiuKey Laboratory of Plant Carbon Capture, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, China.ORCID 0009-0008-3066-797X
Yuan ChenKey Laboratory of Plant Carbon Capture, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, China.
Xue ZhangKey Laboratory of Plant Carbon Capture, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0003-3138-6295
Mengxue LiKey Laboratory of Plant Carbon Capture, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, China.
Ji WangKey Laboratory of Plant Carbon Capture, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, China.
Zhao YangKey Laboratory of Plant Carbon Capture, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0002-5239-4000
Miaolian MaKey Laboratory of Plant Carbon Capture, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, China.ORCID 0009-0007-0085-956X
Zhiwei ZhaoNational Key Laboratory of Plant Molecular Genetics, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0001-5624-3886
Hongtao LiuNational Key Laboratory of Plant Molecular Genetics, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0002-6363-7450
Fang YuShanghai Normal University, Shanghai, China.ORCID 0000-0002-8562-1046
Peng ZhangKey Laboratory of Plant Carbon Capture, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0003-0408-2923

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant cuticular waxes, crucial hydrophobic barriers, are primarily composed of aliphatics derived from very-long-chain fatty acids (VLCFAs; >C28) synthesized by the endoplasmic reticulum fatty acid elongase complex. The core catalytic subunit, CER6 (KCS6), requires interaction with the BAHD protein GL2 to elongate acyl chains beyond C28. We determined the cryo-electron microscopy structure of the maize CER6-GL2 (ZmCER6-ZmGL2) heterotetramer bound to coenzyme A (CoA) and malonyl-CoA, revealing a membrane-anchored ZmCER6 homodimer, with each cytosolic catalytic domain having a substrate tunnel. Structural and biochemical analyses suggest that ZmGL2's amino terminus binds ZmCER6 and remodels its substrate tunnel into a continuous hydrophobic channel at their interface, enabling acyl-chain elongation. CER6 uses a distinct Cys-His-Asn catalytic triad, differing from the histidine-dependent catalysis of mammalian elongases. GL2 acts noncatalytically to modulate CER6 activity. Comparative analyses suggest that species-specific substrate preferences arise from divergent CER2/GL2 interactions. This work elucidates the acyl-chain elongation mechanism of plant VLCFA biosynthesis and provides a foundation for engineering stress-resilient crops via wax modulation.

Indexed as

Fatty AcidsPlant ProteinsWaxesZea maysCatalytic DomainCryoelectron MicroscopyFatty Acid ElongasesModels, MolecularProtein BindingSubstrate SpecificityFatty Acid ElongasesFatty AcidsPlant ProteinsWaxes

Identifiers

PMID41337596
PMCPMC12674111

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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.