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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Rangl M,Miyagi A,Kowal J,Stahlberg H,Nimigean CM,Scheuring Sdoi
10.1038/ncomms12789subject
Has Abstractpub_date
2016-09-20 00:00:00pages
12789issn
2041-1723pii
ncomms12789journal_volume
7pub_type
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