ArticleThe Plant cell2012
Lotus japonicus E3 ligase SEVEN IN ABSENTIA4 destabilizes the symbiosis receptor-like kinase SYMRK and negatively regulates rhizobial infection.
Article in The Plant cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 91 citations in OpenAlex.
- Ubiquitination as a multi-layer regulatory network in legume-rhizobium symbiosis.Plant cell reports · 2026Review
- A LjBAK1-associated E3 ubiquitin ligase, LjPUB7, negatively regulates early symbiosis by targeting NFRs.BMC plant biology · 2025Article
- Receptor-like Kinase GOM1 Regulates Glume-Opening in Rice.Plants (Basel, Switzerland) · 2024Article
- Genome-wide identification of SINA gene family in Medicago truncatula and functional analysis of MtSINAL7.Molecular biology reports · 2024Article
- Genomic-wide analysis reveals seven in absentia genes regulating grain development in wheat (Triticum aestivum L.).The plant genome · 2024Article
- Genome-Wide Identification of Seven in Absentia E3 Ubiquitin Ligase Gene Family and Expression Profiles in Response to Different Hormones inInternational journal of molecular sciences · 2024Article
- Article
- Rice SIAH E3 Ligases Interact with RMD Formin and Affect Plant Morphology.Rice (New York, N.Y.) · 2022Article
- QTL mapping and candidate gene mining of flag leaf size traits in Japonica rice based on linkage mapping and genome-wide association study.Molecular biology reports · 2022Article
- Reciprocal antagonistic regulation of E3 ligases controls ACC synthase stability and responses to stress.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A study of RNA-editing inForestry research · 2021Article
- Receptor-Like Kinases Sustain Symbiotic Scrutiny.Plant physiology · 2020Review
- How to Inactivate Human Ubiquitin E3 Ligases by Mutation.Frontiers in cell and developmental biology · 2020Review
- TheFrontiers in plant science · 2020Article
- Genome-Wide Identification of Apple Ubiquitin SINA E3 Ligase and Functional Characterization of MdSINA2.Frontiers in plant science · 2020Article
- A Lotus japonicus E3 ligase interacts with the Nod Factor Receptor 5 and positively regulates nodulation.BMC plant biology · 2018Article
- Article
- The MtDMI2-MtPUB2 Negative Feedback Loop Plays a Role in Nodulation Homeostasis.Plant physiology · 2018Article
- An Efficient Protocol for Model Legume Root Protoplast Isolation and Transformation.Frontiers in plant science · 2018Article
- Identification of the phosphorylation targets of symbiotic receptor-like kinases using a high-throughput multiplexed assay for kinase specificity.The Plant journal : for cell and molecular biology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Lotus japonicus SYMBIOSIS RECEPTOR-LIKE KINASE (SYMRK) is required for symbiotic signal transduction upon stimulation of root cells by microbial signaling molecules. Here, we identified members of the SEVEN IN ABSENTIA (SINA) E3 ubiquitin-ligase family as SYMRK interactors and confirmed their predicted ubiquitin-ligase activity. In Nicotiana benthamiana leaves, SYMRK-yellow fluorescent protein was localized at the plasma membrane, and interaction with SINAs, as determined by bimolecular fluorescence complementation, was observed in small punctae at the cytosolic interface of the plasma membrane. Moreover, fluorescence-tagged SINA4 partially colocalized with SYMRK and caused SYMRK relocalization as well as disappearance of SYMRK from the plasma membrane. Neither the localization nor the abundance of Nod-factor receptor1 was altered by the presence of SINA4. SINA4 was transcriptionally upregulated during root symbiosis, and rhizobia inoculated roots ectopically expressing SINA4 showed reduced SYMRK protein levels. In accordance with a negative regulatory role in symbiosis, infection thread development was impaired upon ectopic expression of SINA4. Our results implicate SINA4 E3 ubiquitin ligase in the turnover of SYMRK and provide a conceptual mechanism for its symbiosis-appropriate spatio-temporal containment.
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Registered trials
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