ArticleBiophysical journal2004
Assembly of plant Shaker-like K(out) channels requires two distinct sites of the channel alpha-subunit.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 75 citations in OpenAlex.
- GORK KNature communications · 2025Article
- The calcium sensor CBL7 is required for Serendipita indica-induced growth stimulation in Arabidopsis thaliana, controlling defense against the endophyte and KPlant, cell & environment · 2022Article
- Adjustment of KInternational journal of molecular sciences · 2021Review
- The Complex Story of Plant Cyclic Nucleotide-Gated Channels.International journal of molecular sciences · 2021Review
- Isolation and Functional Determination of SKOR Potassium Channel in Purple Osier Willow,International journal of genomics · 2021Article
- Grapevine Potassium Nutrition and Fruit Quality in the Context of Climate Change.Frontiers in plant science · 2020Review
- Article
- Unique features of the grapevine VvK5.1 channel support novel functions for outward K+ channels in plants.Journal of experimental botany · 2019Article
- Review
- Regulation of KFrontiers in plant science · 2019Review
- Identification of regions responsible for the function of the plant KChannels (Austin, Tex.) · 2017Article
- Calmodulin confers calcium sensitivity to the stability of the distal intracellular assembly domain of Kv7.2 channels.Scientific reports · 2017Article
- The receptor-like pseudokinase MRH1 interacts with the voltage-gated potassium channel AKT2.Scientific reports · 2017Article
- S-type Anion Channels SLAC1 and SLAH3 Function as Essential Negative Regulators of Inward K+ Channels and Stomatal Opening in Arabidopsis.The Plant cell · 2016Article
- Nitrate-Dependent Control of Shoot K Homeostasis by the Nitrate Transporter1/Peptide Transporter Family Member NPF7.3/NRT1.5 and the Stelar K+ Outward Rectifier SKOR in Arabidopsis.Plant physiology · 2015Article
- The subfamily-specific assembly of Eag and Erg K+ channels is determined by both the amino and the carboxyl recognition domains.The Journal of biological chemistry · 2014Article
- Evaluating contribution of ionic, osmotic and oxidative stress components towards salinity tolerance in barley.BMC plant biology · 2014Article
- Distinct amino acids in the C-linker domain of the Arabidopsis K+ channel KAT2 determine its subcellular localization and activity at the plasma membrane.Plant physiology · 2014Article
- Involvement of the S4-S5 linker and the C-linker domain regions to voltage-gating in plant Shaker channels: comparison with animal HCN and Kv channels.Plant signaling & behavior · 2014Review
- A suppressor screen of the chimeric AtCNGC11/12 reveals residues important for intersubunit interactions of cyclic nucleotide-gated ion channels.Plant physiology · 2013Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SKOR and GORK are outward-rectifying plant potassium channels from Arabidopsis thaliana. They belong to the Shaker superfamily of voltage-dependent K(+) channels. Channels of this class are composed of four alpha-subunits and subunit assembly is a prerequisite for channel function. In this study the assembly mechanism of SKOR was investigated using the yeast two-hybrid system and functional assays in Xenopus oocytes and in yeast. We demonstrate that SKOR and GORK physically interact and assemble into heteromeric K(out) channels. Deletion mutants and chimeric proteins generated from SKOR and the K(in) channel alpha-subunit KAT1 revealed that the cytoplasmic C-terminus of SKOR determines channel assembly. Two domains that are crucial for channel assembly were identified: i), a proximal interacting region comprising a putative cyclic nucleotide-binding domain together with 33 amino acids just upstream of this domain, and ii), a distal interacting region showing some resemblance to the K(T) domain of KAT1. Both regions contributed differently to channel assembly. Whereas the proximal interacting region was found to be active on its own, the distal interacting region required an intact proximal interacting region to be active. K(out) alpha-subunits did not assemble with K(in) alpha-subunits because of the absence of interaction between their assembly sites.
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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.