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PUB1, an E3 ubiquitin ligase, which interacts with and is phosphorylated by the LYK3 symbiotic receptor kinase, negatively regulates rhizobial infection and nodulation during the nitrogen-fixing root nodule symbiosis in Medicago truncatula In this study, we show that PUB1 also interacts with and is phosphorylated by DOES NOT MAKE INFECTIONS 2, the key symbiotic receptor kinase of the common symbiosis signaling pathway, required for both the rhizobial and the arbuscular mycorrhizal (AM) endosymbioses. We also show here that PUB1 expression is activated during successive stages of root colonization by Rhizophagus irregularis that is compatible with its interaction with DOES NOT MAKE INFECTIONS 2. Through characterization of a mutant, pub1-1, affected by the E3 ubiquitin ligase activity of PUB1, we have shown that the ubiquitination activity of PUB1 is required to negatively modulate successive stages of infection and development of rhizobial and AM symbioses. In conclusion, PUB1 represents, to our knowledge, a novel common component of symbiotic signaling integrating signal perception through interaction with and phosphorylation by two key symbiotic receptor kinases, and downstream signaling via its ubiquitination activity to fine-tune both rhizobial and AM root endosymbioses.

Original publication




Journal article


Plant physiology

Publication Date





2312 - 2324


Institut National de la Recherche Agronomique, Laboratoire des Interactions Plantes-Microorganismes, UMR441, Castanet-Tolosan F-31326, France (T.V., S.C., C.C, C.R., F.D.C.-N., M.M., T.T., V.G., B.L., J.C., C.H.); Centre National de la Recherche Scientifique, Laboratoire des Interactions Plantes-Microorganismes, UMR2594, Castanet-Tolosan F-31326, France (T.V., S.C., C.C, C.R., F.D.C.-N., M.M., T.T., V.G., B.L., J.C., C.H.); and Institut National de la Recherche Agronomique-UMR1347-Agroecologie AgroSup/Institut National de la Recherche Agronomique/uB, Pôle Génétique & Ecophysiologie GEAPSI, 21065 Dijon France (R.T., C.L.).


Rhizobium, Saccharomyces cerevisiae, Mycorrhizae, Medicago truncatula, Ubiquitin-Protein Ligases, Plant Proteins, Colony Count, Microbial, Symbiosis, Phosphorylation, Ubiquitination, Glomeromycota, Protein Domains