ArticleThe Journal of biological chemistry2015
Competing Lipid-Protein and Protein-Protein Interactions Determine Clustering and Gating Patterns in the Potassium Channel from Streptomyces lividans (KcsA).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Elucidating the role of lipid interactions in stabilizing the membrane protein KcsA.Biophysical journal · 2024Article
- Cardiolipin binding enhances KcsA channel gating via both its specific and dianion-monoanion interchangeable sites.iScience · 2023Article
- High-Resolution Magic Angle Spinning NMR of KcsA in Liposomes: The Highly Mobile C-Terminus.Biomolecules · 2022Article
- An extracellular scaffolding complex confers unusual rectification upon an ionotropic acetylcholine receptor inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Mechanisms and physiological implications of cooperative gating of clustered ion channels.Physiological reviews · 2022Review
- NMR studies of lipid regulation of the KBiochimica et biophysica acta. Biomembranes · 2021Article
- Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020Review
- The influence of membrane bilayer thickness on KcsA channel activity.Channels (Austin, Tex.) · 2019Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Accessibility of Cations to the Selectivity Filter of KcsA in the Inactivated State: An Equilibrium Binding Study.International journal of molecular sciences · 2019Article
- The actions of volatile anesthetics: a new perspective.Acta crystallographica. Section D, Structural biology · 2018Review
- Protein crowding and lipid complexity influence the nanoscale dynamic organization of ion channels in cell membranes.Scientific reports · 2017Article
- Effects of selenium on myocardial apoptosis by modifying the activity of mitochondrial STAT3 and regulating potassium channel expression.Experimental and therapeutic medicine · 2017Article
- Inactivation in the potassium channel KcsA.Journal of structural biology: XArticle
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
There is increasing evidence to support the notion that membrane proteins, instead of being isolated components floating in a fluid lipid environment, can be assembled into supramolecular complexes that take part in a variety of cooperative cellular functions. The interplay between lipid-protein and protein-protein interactions is expected to be a determinant factor in the assembly and dynamics of such membrane complexes. Here we report on a role of anionic phospholipids in determining the extent of clustering of KcsA, a model potassium channel. Assembly/disassembly of channel clusters occurs, at least partly, as a consequence of competing lipid-protein and protein-protein interactions at nonannular lipid binding sites on the channel surface and brings about profound changes in the gating properties of the channel. Our results suggest that these latter effects of anionic lipids are mediated via the Trp(67)-Glu(71)-Asp(80) inactivation triad within the channel structure and its bearing on the selectivity filter.
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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.