ArticleNature communications2016
Real-time visualization of conformational changes within single MloK1 cyclic nucleotide-modulated channels.
Article in Nature communications, 2016. 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, 29 citations in OpenAlex.
- CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021Review
- Recent advances in bioimaging with high-speed atomic force microscopy.Biophysical reviews · 2020Review
- Article
- Advances in high-speed atomic force microscopy (HS-AFM) reveal dynamics of transmembrane channels and transporters.Current opinion in structural biology · 2019Review
- Retrieving high-resolution information from disordered 2D crystals by single-particle cryo-EM.Nature communications · 2019Article
- Structural titration of receptor ion channel GLIC gating by HS-AFM.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- An iris diaphragm mechanism to gate a cyclic nucleotide-gated ion channel.Nature communications · 2018Article
- Lysenin Toxin Membrane Insertion Is pH-Dependent but Independent of Neighboring Lysenins.Biophysical journal · 2017Article
- Directly watching biomolecules in action by high-speed atomic force microscopy.Biophysical reviews · 2017Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic cyclic nucleotide-modulated (CNM) ion channels perform various physiological roles by opening in response to cyclic nucleotides binding to a specialized cyclic nucleotide-binding domain. Despite progress in structure-function analysis, the conformational rearrangements underlying the gating of these channels are still unknown. Here, we image ligand-induced conformational changes in single CNM channels from Mesorhizobium loti (MloK1) in real-time, using high-speed atomic force microscopy. In the presence of cAMP, most channels are in a stable conformation, but a few molecules dynamically switch back and forth (blink) between at least two conformations with different heights. Upon cAMP depletion, more channels start blinking, with blinking heights increasing over time, suggestive of slow, progressive loss of ligands from the tetramer. We propose that during gating, MloK1 transitions from a set of mobile conformations in the absence to a stable conformation in the presence of ligand and that these conformations are central for gating the pore.
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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.