ArticleProceedings of the National Academy of Sciences of the United States of America2011
Locating an extracellular K+-dependent interaction site that modulates betaine-binding of the Na+-coupled betaine symporter BetP.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 37 citations in OpenAlex.
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- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Unraveling antibody-induced mechanical stability of antigen: Insights from single-molecule studies.Protein science : a publication of the Protein Society · 2025Article
- The insertase YidC chaperones the polytopic membrane protein MelB inserting and folding simultaneously from both termini.Structure (London, England : 1993) · 2023Article
- Insights into autoregulation of a membrane protein complex by its cytoplasmic domains.Biophysical journal · 2023Article
- Substrate-binding guides individual melibiose permeases MelB to structurally soften and to destabilize cytoplasmic middle-loop C3.Structure (London, England : 1993) · 2023Article
- Article
- Differences in the mechanical unfolding pathways of apo- and copper-bound azurins.Scientific reports · 2018Article
- The N Terminus Specifies the Switch between Transport Modes of the Human Serotonin Transporter.The Journal of biological chemistry · 2017Article
- Structural Heterogeneity of CNGA1 Channels Revealed by Electrophysiology and Single-Molecule Force Spectroscopy.ACS omega · 2016Article
- YidC assists the stepwise and stochastic folding of membrane proteins.Nature chemical biology · 2016Article
- Molecular Plasticity of the Human Voltage-Dependent Anion Channel Embedded Into a Membrane.Structure (London, England : 1993) · 2016Article
- Conformational rearrangements in the transmembrane domain of CNGA1 channels revealed by single-molecule force spectroscopy.Nature communications · 2015Article
- Observing a lipid-dependent alteration in single lactose permeases.Structure (London, England : 1993) · 2015Article
- Substrate-bound outward-open state of the betaine transporter BetP provides insights into Na+ coupling.Nature communications · 2014Article
- Substrate-induced changes in the structural properties of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.Biochimica et biophysica acta · 2014Review
- Peptide transporter DtpA has two alternate conformations, one of which is promoted by inhibitor binding.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin.Structure (London, England : 1993) · 2013Article
- Cholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BetP, a trimeric Na(+)-coupled betaine symporter, senses hyperosmotic stress via its cytoplasmic C-terminal domain and regulates transport activity in dependence of the cytoplasmic K(+)-concentration. This transport regulation of BetP depends on a sophisticated interaction network. Using single-molecule force spectroscopy we structurally localize and quantify these interactions changing on K(+)-dependent transport activation and substrate-binding. K(+) significantly strengthened all interactions, modulated lifetimes of functionally important structural regions, and increased the mechanical rigidity of the symporter. Substrate-binding could modulate, but not establish most of these K(+)-dependent interactions. A pronounced effect triggered by K(+) was observed at the periplasmic helical loop EH2. Tryptophan quenching experiments revealed that elevated K(+)-concentrations akin to those BetP encounters during hyperosmotic stress trigger the formation of a periplasmic second betaine-binding (S2) site, which was found to be at a similar position reported previously for the BetP homologue CaiT. In BetP, the presence of the S2 site strengthened the interaction between EH2, transmembrane α-helix 12 and the K(+)-sensing C-terminal domain resulting in a K(+)-dependent cooperative betaine-binding.
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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.