Evidence map›Paper›PMID 33955482›Full record

ArticleThe Plant cell2021

UGT76B1, a promiscuous hub of small molecule-based immune signaling, glucosylates N-hydroxypipecolic acid, and balances plant immunity.

Sibylle Bauer, Dereje W Mekonnen, Michael Hartmann, Ipek Yildiz, Robert Janowski, Birgit Lange, Birgit Geist, Jürgen Zeier, Anton R Schäffner

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
14.6field-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

51 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cysteine Signalling in Plant Pathogen Response.Plant, cell & environment · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The Analysis of the Glycosyltransferase Activity Gene Family inInternational journal of molecular sciences · 2025
    Article
  17. Review
  18. Review
  19. Article
  20. Article
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

9 authors at 2 institutions in 1 country.

Sibylle BauerDepartment of Environmental Sciences, Institute of Biochemical Plant Pathology, Helmholtz Zentrum München, München, Germany.ORCID 0000-0001-5501-7481
Dereje W MekonnenDepartment of Environmental Sciences, Institute of Biochemical Plant Pathology, Helmholtz Zentrum München, München, Germany.ORCID 0000-0003-3167-7412
Michael HartmannDepartment of Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.ORCID 0000-0003-4828-958X
Ipek YildizDepartment of Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.ORCID 0000-0002-9949-0358
Robert JanowskiIntracellular Transport and RNA Biology Group, Institute of Structural Biology, Helmholtz Zentrum München, München, Germany.ORCID 0000-0002-9940-2143
Birgit LangeDepartment of Environmental Sciences, Institute of Biochemical Plant Pathology, Helmholtz Zentrum München, München, Germany.ORCID 0000-0002-2332-9154
Birgit GeistDepartment of Environmental Sciences, Institute of Biochemical Plant Pathology, Helmholtz Zentrum München, München, Germany.ORCID 0000-0002-1996-6177
Jürgen ZeierDepartment of Biology, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.ORCID 0000-0002-8703-5403
Anton R SchäffnerDepartment of Environmental Sciences, Institute of Biochemical Plant Pathology, Helmholtz Zentrum München, München, Germany.ORCID 0000-0002-9424-5548
Helmholtz Zentrum München · DEHeinrich Heine University Düsseldorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glucosylation modulates the biological activity of small molecules and frequently leads to their inactivation. The Arabidopsis thaliana glucosyltransferase UGT76B1 is involved in conjugating the stress hormone salicylic acid (SA) as well as isoleucic acid (ILA). Here, we show that UGT76B1 also glucosylates N-hydroxypipecolic acid (NHP), which is synthesized by FLAVIN-DEPENDENT MONOOXYGENASE 1 (FMO1) and activates systemic acquired resistance (SAR). Upon pathogen attack, Arabidopsis leaves generate two distinct NHP hexose conjugates, NHP-O-β-glucoside and NHP glucose ester, whereupon only NHP-O-β-glucoside formation requires a functional SA pathway. The ugt76b1 mutants specifically fail to generate the NHP-O-β-glucoside, and recombinant UGT76B1 synthesizes NHP-O-β-glucoside in vitro in competition with SA and ILA. The loss of UGT76B1 elevates the endogenous levels of NHP, SA, and ILA and establishes a constitutive SAR-like immune status. Introgression of the fmo1 mutant lacking NHP biosynthesis into the ugt76b1 background abolishes this SAR-like resistance. Moreover, overexpression of UGT76B1 in Arabidopsis shifts the NHP and SA pools toward O-β-glucoside formation and abrogates pathogen-induced SAR. Our results further indicate that NHP-triggered immunity is SA-dependent and relies on UGT76B1 as a common metabolic hub. Thereby, UGT76B1-mediated glucosylation controls the levels of active NHP, SA, and ILA in concert to balance the plant immune status.

Indexed as

ArabidopsisArabidopsis ProteinsGlycosyltransferasesPipecolic AcidsPlant ImmunityArabidopsis ProteinsGlycosyltransferasesN-hydroxypipecolic acidPipecolic AcidsUGT76B1 protein, Arabidopsis

Identifiers

PMID33955482
PMCPMC8136890
OpenAlexW3150545901

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.