ArticlePlant physiology2011
TNO1 is involved in salt tolerance and vacuolar trafficking in Arabidopsis.
Article in Plant physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 53 citations in OpenAlex.
- Plant-specific tail-anchored coiled-coil protein MAG3 stabilizes Golgi-associated ERESs to facilitate protein exit from the ER.Communications biology · 2025Article
- Regulation of adaptive growth decisions via phosphorylation of the TRAPPII complex in Arabidopsis.The Journal of cell biology · 2024Article
- Genetic Architecture of Salt Tolerance in Cowpea (International journal of molecular sciences · 2023Article
- Genome-Wide Analysis of the SNARE Family in Cultivated Peanut (International journal of molecular sciences · 2023Article
- Genomic evidence for homoploid hybrid speciation between ancestors of two different genera.Nature communications · 2022Article
- The TGN/EE SNARE protein SYP61 and the ubiquitin ligase ATL31 cooperatively regulate plant responses to carbon/nitrogen conditions in Arabidopsis.The Plant cell · 2022Article
- Genetic architecture of salt tolerance in a Multi-Parent Advanced Generation Inter-Cross (MAGIC) cowpea population.BMC genomics · 2022Article
- An Update on the Key Factors Required for Plant Golgi Structure Maintenance.Frontiers in plant science · 2022Review
- Multiple functions of the vacuole in plant growth and fruit quality.Molecular horticulture · 2021Review
- Current Understanding of Role of Vesicular Transport in Salt Secretion by Salt Glands in Recretohalophytes.International journal of molecular sciences · 2021Review
- Heat Stress-Dependent Association of Membrane Trafficking Proteins With mRNPs Is Selective.Frontiers in plant science · 2021Article
- SNAREs in Plant Biotic and Abiotic Stress Responses.Molecules and cells · 2020Review
- Loss ofFrontiers in plant science · 2020Article
- AtTRAPPC11/ROG2: A Role for TRAPPs in Maintenance of the PlantThe Plant cell · 2019Article
- Global profiling of alternative splicing landscape responsive to drought, heat and their combination in wheat (Triticum aestivum L.).Plant biotechnology journal · 2018Article
- Post-Golgi Trafficking and Transport of Cell Wall Components.Frontiers in plant science · 2018Review
- The Plant Trans-Golgi Network: Not Just a Matter of Distinction.Plant physiology · 2018Review
- TNO1, a TGN-localized SNARE-interacting protein, modulates root skewing in Arabidopsis thaliana.BMC plant biology · 2017Article
- A SNARE-Like Superfamily Protein SbSLSP from the Halophyte Salicornia brachiata Confers Salt and Drought Tolerance by Maintaining Membrane Stability, K(+)/Na(+) Ratio, and Antioxidant Machinery.Frontiers in plant science · 2016Article
- Grapevine and Arabidopsis Cation-Chloride Cotransporters Localize to the Golgi and Trans-Golgi Network and Indirectly Influence Long-Distance Ion Transport and Plant Salt Tolerance.Plant physiology · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Arabidopsis (Arabidopsis thaliana) soluble N-ethylmaleimide-sensitive factor attachment protein receptor SYP41 is involved in vesicle fusion at the trans-Golgi network (TGN) and interacts with AtVPS45, SYP61, and VTI12. These proteins are involved in diverse cellular processes, including vacuole biogenesis and stress tolerance. A previously uncharacterized protein, named TNO1 (for TGN-localized SYP41-interacting protein), was identified by coimmunoprecipitation as a SYP41-interacting protein. TNO1 was found to localize to the TGN by immunofluorescence microscopy. A tno1 mutant showed increased sensitivity to high concentrations of NaCl, KCl, and LiCl and also to mannitol-induced osmotic stress. Localization of SYP61, which is involved in the salt stress response, was disrupted in the tno1 mutant. Vacuolar proteins were partially secreted to the apoplast in the tno1 mutant, suggesting that TNO1 is required for efficient protein trafficking to the vacuole. The tno1 mutant had delayed formation of the brefeldin A (BFA) compartment in cotyledons upon application of BFA, suggesting less efficient membrane fusion processes in the mutant. Unlike most TGN proteins, TNO1 does not relocate to the BFA compartment upon BFA treatment. These data demonstrate that TNO1 is involved in vacuolar trafficking and salt tolerance, potentially via roles in vesicle fusion and in maintaining TGN structure or identity.
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