ArticleProceedings of the National Academy of Sciences of the United States of America2002
The carboxyl tail forms a discrete functional domain that blocks closure of the yeast K+ channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Molecular architecture of the fungal-specific potassium channel TOK1.Nature communications · 2026Article
- TOK channels use the two gates in classical KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Promising Antifungal Targets AgainstFrontiers in cellular and infection microbiology · 2018Review
- Article
- Ion channels in microbes.Physiological reviews · 2008Review
- Interactive domains between pore loops of the yeast K+ channel TOK1 associate with extracellular K+ sensitivity.The Biochemical journal · 2006Article
- Ability of Sit4p to promote K+ efflux via Nha1p is modulated by Sap155p and Sap185p.Eukaryotic cell · 2005Article
- Microbial K+ channels.The Journal of general physiology · 2005Review
- TOK homologue in Neurospora crassa: first cloning and functional characterization of an ion channel in a filamentous fungus.Eukaryotic cell · 2003Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Non-targeted mutagenesis studies of the yeast K(+) channel, TOK1, have led to identification of functional domains common to other cation channels as well as those so far not found in other channels. Among the latter is the ability of the carboxyl tail to prevent channel closure. Here, we show that the tail can fulfill this function in trans. Coexpression of the carboxyl tail with the tail-deleted channel core restores normal channel behavior A Ser/Thr-rich region at its amino end and an acidic stretch at its carboxyl end delineate the minimal region required for tail function. This region of 160 aa apparently forms a discrete functional domain. Interaction of this domain with the channel core is strong, being recalcitrant to removal from excised membrane patches by both high salt and reducing agents. Although the use of a cytoplasmic domain to regulate channel is common among animal channels, by using it as a "foot-in-the-door" to maintain open state appears unique to TOK1, the first fungal K(+) channel studied in depth.
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