ArticlePlant physiology2012
The ubiquitin E3 ligase LOSS OF GDU2 is required for GLUTAMINE DUMPER1-induced amino acid secretion in Arabidopsis.
Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Exl1 from Pectobacterium activates a jasmonate-dependent immune network in Arabidopsis thaliana.Plant molecular biology · 2026Article
- Hormonal and transcriptomic regulation of drought adaptation in barley roots and leaves.Scientific reports · 2025Article
- PANTOTHENATE KINASE4, LOSS OF GDU2, and TRANSPOSON PROTEIN1 affect the canalization of tomato fruit metabolism.Plant physiology · 2023Article
- Functional Characterization of PotatoInternational journal of molecular sciences · 2023Article
- Novel candidate genes for lignin structure identified through genome-wide association study of naturally varyingFrontiers in plant science · 2023Article
- RING Zinc Finger Proteins in Plant Abiotic Stress Tolerance.Frontiers in plant science · 2022Review
- The F-box E3 ubiquitin ligase BAF1 mediates the degradation of the brassinosteroid-activated transcription factor BES1 through selective autophagy in Arabidopsis.The Plant cell · 2021Article
- Transcriptomic analysis of differentially expressed genes in leaves and roots of two alfalfa (Medicago sativa L.) cultivars with different salt tolerance.BMC plant biology · 2021Article
- Ubiquitylation of ABA Receptors and Protein Phosphatase 2C Coreceptors to Modulate ABA Signaling and Stress Response.International journal of molecular sciences · 2021Review
- The Ubiquitin E3 Ligase MaLUL2 Is Involved in High Temperature-Induced Green Ripening in Banana Fruit.International journal of molecular sciences · 2020Article
- The Transcription Factor EIL1 Participates in the Regulation of Sulfur-Deficiency Response.Plant physiology · 2020Article
- The UBC27-AIRP3 ubiquitination complex modulates ABA signaling by promoting the degradation of ABI1 in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Proteasomal Degradation of Proteins Is Important for the Proper Transcriptional Response to Sulfur Deficiency Conditions in Plants.Plant & cell physiology · 2020Article
- Increased Expression of UMAMIT Amino Acid Transporters Results in Activation of Salicylic Acid Dependent Stress Response.Frontiers in plant science · 2020Article
- Loci and candidate genes controlling root traits in wheat seedlings-a wheat root GWAS.Functional & integrative genomics · 2019Article
- Arabidopsis UMAMIT24 and 25 are amino acid exporters involved in seed loading.Journal of experimental botany · 2018Article
- Targeted Profiling ofThe Plant cell · 2018Article
- AtAIRP2 E3 Ligase Affects ABA and High-Salinity Responses by Stimulating Its ATP1/SDIRIP1 Substrate Turnover.Plant physiology · 2017Article
- Selective Autophagy of BES1 Mediated by DSK2 Balances Plant Growth and Survival.Developmental cell · 2017Article
- Control of Amino Acid Homeostasis by a Ubiquitin Ligase-Coactivator Protein Complex.The Journal of biological chemistry · 2017Article
Corrections and comments
- Erratum issued
Authors and funding
8 authors.
Funding
Abstract
Amino acids serve as transport forms for organic nitrogen in the plant, and multiple transport steps are involved in cellular import and export. While the nature of the export mechanism is unknown, overexpression of GLUTAMINE DUMPER1 (GDU1) in Arabidopsis (Arabidopsis thaliana) led to increased amino acid export. To gain insight into GDU1's role, we searched for ethyl-methanesulfonate suppressor mutants and performed yeast-two-hybrid screens. Both methods uncovered the same gene, LOSS OF GDU2 (LOG2), which encodes a RING-type E3 ubiquitin ligase. The interaction between LOG2 and GDU1 was confirmed by glutathione S-transferase pull-down, in vitro ubiquitination, and in planta coimmunoprecipitation experiments. Confocal microscopy and subcellular fractionation indicated that LOG2 and GDU1 both localized to membranes and were enriched at the plasma membrane. LOG2 expression overlapped with GDU1 in the xylem and phloem tissues of Arabidopsis. The GDU1 protein encoded by the previously characterized intragenic suppressor mutant log1-1, with an arginine in place of a conserved glycine, failed to interact in the multiple assays, suggesting that the Gdu1D phenotype requires the interaction of GDU1 with LOG2. This hypothesis was supported by suppression of the Gdu1D phenotype after reduction of LOG2 expression using either artificial microRNAs or a LOG2 T-DNA insertion. Altogether, in accordance with the emerging bulk of data showing membrane protein regulation via ubiquitination, these data suggest that the interaction of GDU1 and the ubiquitin ligase LOG2 plays a significant role in the regulation of amino acid export from plant cells.
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