ArticleThe Plant cell2015
The Arabidopsis R-SNARE VAMP721 Interacts with KAT1 and KC1 K+ Channels to Moderate K+ Current at the Plasma Membrane.
Article in The Plant cell, 2015. 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 57 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
57 citing papers in PubMed, 100 citations in OpenAlex.
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- Genetic markers of stomatal cluster development in Begoniaceae revealed through trait analysis assisted by interactive deep-learning.Plant physiology · 2026Article
- Genome-Wide Identification and Characterization of Stress-Responsive SNARE Genes in Quinoa (Biology · 2026Article
- The 14-3-3 protein nt GF14e interacts with CIPK2 and increases low potassium stress in tobacco.Plant signaling & behavior · 2024Article
- SYNTAXIN OF PLANTS 132 underpins secretion of cargoes associated with salicylic acid signaling and pathogen defense.Plant physiology · 2024Article
- The nonphototrophic hypocotyl 3 (NPH3) domain protein NRL5 is a trafficking-associated GTPase essential for drought resistance.Science advances · 2024Article
- Article
- ER Membrane Protein Interactions Using the Split-Ubiquitin System (SUS).Methods in molecular biology (Clifton, N.J.) · 2024Article
- 2 in 1 Vectors Improve in Planta BiFC and FRET Analysis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- VAMP726 and VAMP725 regulate vesicle secretion and pollen tube growth in Arabidopsis.Plant cell reports · 2023Article
- VAMP726 from maize and Arabidopsis confers pollen resistance to heat and UV radiation by influencing lignin content of sporopollenin.Plant communications · 2023Article
- VAMP724 and VAMP726 are involved in autophagosome formation inAutophagy · 2023Article
- Characterization of BananaPlants (Basel, Switzerland) · 2023Article
- Analyzing Protein-Protein Interactions Using the Split-Ubiquitin System.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Genome-wide identification ofFrontiers in plant science · 2023Article
- Transcriptional network underpinning ploidy-related elevated leaf potassium in neo-tetraploids.Plant physiology · 2022Article
- SNARE SYP132 mediates divergent traffic of plasma membrane H+-ATPase AHA1 and antimicrobial PR1 during bacterial pathogenesis.Plant physiology · 2022Article
- Transcription Profile of Auxin Related Genes during Positively Gravitropic Hypocotyl Curvature ofPlants (Basel, Switzerland) · 2022Article
- Non-autonomous stomatal control by pavement cell turgor via the K+ channel subunit AtKC1.The Plant cell · 2022Article
Corrections and comments
- Erratum issuedCorrection.2015
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
SNARE (soluble N-ethylmaleimide-sensitive factor protein attachment protein receptor) proteins drive vesicle traffic, delivering membrane and cargo to target sites within the cell and at its surface. They contribute to cell homeostasis, morphogenesis, and pathogen defense. A subset of SNAREs, including the Arabidopsis thaliana SNARE SYP121, are known also to coordinate solute uptake via physical interactions with K(+) channels and to moderate their gating at the plasma membrane. Here, we identify a second subset of SNAREs that interact to control these K(+) channels, but with opposing actions on gating. We show that VAMPs (vesicle-associated membrane proteins), which target vesicles to the plasma membrane, also interact with and suppress the activities of the inward-rectifying K(+) channels KAT1 and KC1. Interactions were evident in yeast split-ubiquitin assays, they were recovered in vivo by ratiometric bimolecular fluorescence complementation, and they were sensitive to mutation of a single residue, Tyr-57, within the longin domain of VAMP721. Interaction was also recovered on exchange of the residue at this site in the homolog VAMP723, which normally localizes to the endoplasmic reticulum and otherwise did not interact. Functional analysis showed reduced channel activity and alterations in voltage sensitivity that are best explained by a physical interaction with the channel gates. These actions complement those of SYP121, a cognate SNARE partner of VAMP721, and lead us to propose that the channel interactions reflect a "hand-off" in channel control between the two SNARE proteins that is woven together with vesicle fusion.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.