LiP-MS reveals a feedback loop of tomato UDP-glucosyltransferases managing bioactive jasmonate homeostasis
8 affiliations
- 1Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium
- 2VIB Center for Plant Systems Biology, 9052 Ghent, Belgium
- 3Department of Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences, University of Goettingen, 37077 Goettingen, Germany
- 4Department of Organic and Macromolecular Chemistry, Ghent University, 9000 Ghent, Belgium
- 5Laboratory of Integrative Metabolomics (LIMET), Department of Translational Physiology, Infectiology and Public Health, Ghent University, 9820 Merelbeke, Belgium
- 6iRIP Unit, Laboratory of Microbiology, Department of Biochemistry and Microbiology, Ghent University, 9000 Ghent, Belgium
- 7Department of Plant Biochemistry, Goettingen Center for Molecular Biosciences (GZMB), University of Goettingen, 37077 Goettingen, Germany
- 8Department of Botany and Zoology, Stellenbosch University, Private Bag X1, Matieland 7600, South Africa
Abstract
Jasmonic acid (JA) is the precursor of the bioactive molecule jasmonoyl-isoleucine (JA-Ile), a plant hormone that regulates fitness and development. Although JA biosynthesis, signaling, and responses have been intensively studied, the catabolism of JA remains incompletely understood. Here, we use the recently developed technique of limited proteolysis-coupled mass spectrometry (LiP-MS) to investigate metabolite-protein interactions in plants, aiming to discover enzymes involved in JA metabolism. We identify several previously reported JA-binding proteins, thus validating the robustness of the method, along with recognized enzymes of the JA pathway and a series of other potential JA-binding proteins. Functional characterization of a set of identified JA-interacting uridine diphosphate (UDP)-glycosyltransferase (UGT) enzymes through omics, biochemical, enzymatic, and structural analyses reveals that two tomato UGTs glucosylate JA into JA-glucosyl esters, potentially playing a role in the regulation of bioactive JA homeostasis. With this, our findings uncover a missing step in the JA metabolic pathway.
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BibTeX
@article{venegasmolina2026lipms,
title = {{LiP-MS reveals a feedback loop of tomato UDP-glucosyltransferases managing bioactive jasmonate homeostasis}},
author = {Jhon Venegas-Molina and Lennart Mohnike and Sara Selma García and Hilde Janssens and José Diana Di Mavungu and Kaylan Reddy and Robin Colembie and Issl Kimpe and Ana Cristina Jaramillo-Madrid and Elia Lacchini and Lynn Vanhaecke and Johan M. Winne and Petra Van Damme and Ivo Feussner and Alain Goossens and Krešimir Šola},
journal = {Cell Reports},
year = {2026},
month = sep,
doi = {10.1016/j.celrep.2026.118034},
url = {https://doi.org/10.1016/j.celrep.2026.118034},
note = {CC BY-NC 4.0},
}
RIS
TY - JOUR
TI - LiP-MS reveals a feedback loop of tomato UDP-glucosyltransferases managing bioactive jasmonate homeostasis
AU - Jhon Venegas-Molina
AU - Lennart Mohnike
AU - Sara Selma García
AU - Hilde Janssens
AU - José Diana Di Mavungu
AU - Kaylan Reddy
AU - Robin Colembie
AU - Issl Kimpe
AU - Ana Cristina Jaramillo-Madrid
AU - Elia Lacchini
AU - Lynn Vanhaecke
AU - Johan M. Winne
AU - Petra Van Damme
AU - Ivo Feussner
AU - Alain Goossens
AU - Krešimir Šola
PY - 2026
DA - 2026/09/25
JO - Cell Reports
DO - 10.1016/j.celrep.2026.118034
UR - https://doi.org/10.1016/j.celrep.2026.118034
AB - Jasmonic acid (JA) is the precursor of the bioactive molecule jasmonoyl-isoleucine (JA-Ile), a plant hormone that regulates fitness and development. Although JA biosynthesis, signaling, and responses have been intensively studied, the catabolism of JA remains incompletely understood. Here, we use the recently developed technique of limited proteolysis-coupled mass spectrometry (LiP-MS) to investigate metabolite-protein interactions in plants, aiming to discover enzymes involved in JA metabolism. We identify several previously reported JA-binding proteins, thus validating the robustness of the method, along with recognized enzymes of the JA pathway and a series of other potential JA-binding proteins. Functional characterization of a set of identified JA-interacting uridine diphosphate (UDP)-glycosyltransferase (UGT) enzymes through omics, biochemical, enzymatic, and structural analyses reveals that two tomato UGTs glucosylate JA into JA-glucosyl esters, potentially playing a role in the regulation of bioactive JA homeostasis. With this, our findings uncover a missing step in the JA metabolic pathway.
SN - 2211-1247
ER -