ArticleProceedings of the National Academy of Sciences of the United States of America2007
Contribution of hydrophobic and electrostatic interactions to the membrane integration of the Shaker K+ channel voltage sensor domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- The Molecular Biodiversity of Protein Targeting and Protein Transport Related to the Endoplasmic Reticulum.International journal of molecular sciences · 2021Review
- Folding and Insertion of Transmembrane Helices at the ER.International journal of molecular sciences · 2021Review
- Ubiquitination of disease-causing CFTR variants in a microsome-based assay.Analytical biochemistry · 2020Article
- Harmonizing Experimental Data with Modeling to Predict Membrane Protein Insertion in Yeast.Biophysical journal · 2019Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- A Shared Mechanism for the Folding of Voltage-Gated KBiochemistry · 2019Article
- Functional characterization of Kv11.1 (hERG) potassium channels split in the voltage-sensing domain.Pflugers Archiv : European journal of physiology · 2018Article
- Identifying ionic interactions within a membrane using BLaTM, a genetic tool to measure homo- and heterotypic transmembrane helix-helix interactions.Scientific reports · 2017Article
- Transmural gradients in ion channel and auxiliary subunit expression.Progress in biophysics and molecular biology · 2016Review
- Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.Protein science : a publication of the Protein Society · 2015Review
- Voltage Sensing in Membranes: From Macroscopic Currents to Molecular Motions.The Journal of membrane biology · 2015Review
- Mechanisms of integral membrane protein insertion and folding.Journal of molecular biology · 2015Review
- Large-scale mutational analysis of Kv11.1 reveals molecular insights into type 2 long QT syndrome.Nature communications · 2014Article
- Type II transmembrane domain hydrophobicity dictates the cotranslational dependence for inversion.Molecular biology of the cell · 2014Article
- Life at the border: adaptation of proteins to anisotropic membrane environment.Protein science : a publication of the Protein Society · 2014Review
- Asymmetric functional contributions of acidic and aromatic side chains in sodium channel voltage-sensor domains.The Journal of general physiology · 2014Article
- Transmembrane segments form tertiary hairpins in the folding vestibule of the ribosome.Journal of molecular biology · 2014Article
- Article
- Surface expression and channel function of TRPM8 are cooperatively controlled by transmembrane segments S3 and S4.Pflugers Archiv : European journal of physiology · 2013Article
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8 authors.
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Abstract
Membrane-embedded voltage-sensor domains in voltage-dependent potassium channels (K(v) channels) contain an impressive number of charged residues. How can such highly charged protein domains be efficiently inserted into biological membranes? In the plant K(v) channel KAT1, the S2, S3, and S4 transmembrane helices insert cooperatively, because the S3, S4, and S3-S4 segments do not have any membrane insertion ability by themselves. Here we show that, in the Drosophila Shaker K(v) channel, which has a more hydrophobic S3 helix than KAT1, S3 can both insert into the membrane by itself and mediate the insertion of the S3-S4 segment in the absence of S2. An engineered KAT1 S3-S4 segment in which the hydrophobicity of S3 was increased or where S3 was replaced by Shaker S3 behaves as Shaker S3-S4. Electrostatic interactions among charged residues in S2, S3, and S4, including the salt bridges between E283 or E293 in S2 and R368 in S4, are required for fully efficient membrane insertion of the Shaker voltage-sensor domain. These results suggest that cooperative insertion of the voltage-sensor transmembrane helices is a property common to K(v) channels and that the degree of cooperativity depends on a balance between electrostatic and hydrophobic forces.
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