ArticleThe Journal of membrane biology2011
Do small headgroups of phosphatidylethanolamine and phosphatidic acid lead to a similar folding pattern of the K(+) channel?
Article in The Journal of membrane biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Cryo-EM structures of human ABCA7 provide insights into its phospholipid translocation mechanisms.The EMBO journal · 2023Article
- Remodeling of the Plasma Membrane by Surface-Bound Protein Monomers and Oligomers: The Critical Role of Intrinsically Disordered Regions.The Journal of membrane biology · 2022Review
- Plant-derived extracellular vesicles: a novel nanomedicine approach with advantages and challenges.Cell communication and signaling : CCS · 2022Review
- New Insights Into the Antibacterial Mechanism of Cryptotanshinone, a Representative Diterpenoid Quinone FromFrontiers in microbiology · 2021Article
- Role of Lipid Composition in the Interaction and Activity of the Antimicrobial Compound Fengycin with Complex Membrane Models.The Journal of membrane biology · 2019Article
- Diminishing the side effect of mitomycin C by using pH-sensitive liposomes: in vitro characterization and in vivo pharmacokinetics.Drug design, development and therapy · 2018Article
- Special interaction of anionic phosphatidic acid promotes high secondary structure in tetrameric potassium channel.The Journal of membrane biology · 2014Article
- Mimicking the mechanical properties of the cell cortex by the self-assembly of an actin cortex in vesicles.Applied physics letters · 2014Article
- Membrane lipids in Agrobacterium tumefaciens: biosynthetic pathways and importance for pathogenesis.Frontiers in plant science · 2014Review
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phospholipid headgroups act as major determinants in proper folding of oligomeric membrane proteins. The K(+)-channel KcsA is the most popular model protein among these complexes. The presence of zwitterionic nonbilayer lipid phosphatidylethanolamine (PE) is crucial for efficient tetramerization and stabilization of KcsA in a lipid bilayer. In this study, the influence of PE on KcsA folding properties was analyzed by tryptophan fluorescence and acrylamide quenching experiments and compared with the effect of anionic phosphatidic acid (PA). The preliminary studies suggest that the small size and hydrogen bonding capability of the PE headgroup influences KcsA folding via a mechanism quite similar to that observed for anionic PA.
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