Real-time visualization of conformational changes within single MloK1 cyclic nucleotide-modulated channels

Martina Rangl, Atsushi Miyagi, Julia Kowal, Henning Stahlberg, Crina M. Nimigean () and Simon Scheuring ()
Additional contact information
Martina Rangl: INSERM U1006, Aix-Marseille Université, Parc Scientifique et Technologique de Luminy
Atsushi Miyagi: INSERM U1006, Aix-Marseille Université, Parc Scientifique et Technologique de Luminy
Julia Kowal: Center for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel
Henning Stahlberg: Center for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel
Crina M. Nimigean: INSERM U1006, Aix-Marseille Université, Parc Scientifique et Technologique de Luminy
Simon Scheuring: INSERM U1006, Aix-Marseille Université, Parc Scientifique et Technologique de Luminy

Nature Communications, 2016, vol. 7, issue 1, 1-8

Abstract: 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.

Date: 2016
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms12789 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12789

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms12789

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().