Aug 2026· Biochemical Society Transactions· Vol 54, pp. 1095 - 1106· 0 citations· 105 references
Medicine
TL;DR
The binding sites of the channel for various ligands/modulators are highlighted, and an emerging model focusing on the structural rearrangements associated with the transition of the channel from the closed/deactivated to open/activated conformation during lipid-dependent gating is provided which should be broadly applicable to all Kir channels.
Abstract
Abstract Inward-rectifying K+ (Kir) channels are ubiquitously present in variety of cells and play an important role in maintaining resting membrane potential and supporting K+ homeostasis. They are an important family of K+ channels that connects cellular metabolism to membrane excitability, and exhibit complex lipid–protein interaction landscape. Dysfunction of Kir channels is, therefore, associated with multi-factorial diseases and are important drug targets. Recent high-resolution structural dynamics and functional studies of several Kir channels have significantly advanced our understanding of the mechanisms of voltage-dependent pore block and channel gating regulation mediated by lipids, and other modulators. In the present minireview, based on recent knowledge derived from prokaryotic and eukaryotic Kir channels, we highlight the binding sites of the channel for various ligands/modulators, and also provide an emerging model focusing on the structural rearrangements associated with the transition of the channel from the closed/deactivated to open/activated conformation during lipid-dependent gating, which should be broadly applicable to all Kir channels.
Novel mechanistic insights are provided into the molecular mechanisms governing Kv7 channel modulation by exogenous ligands which may prove useful to target Kv7 channels with more potent and selective modulators.
T. Ciaglia, G. Carleo, Zhenni Yang et al.· Angewandte Chemie· 0 citations
It is argued that the central challenge is no longer simply to activate or inhibit TRPM4, but to stabilize the right conformational state in the right tissue at the right stage of pathology.
I. Araya-Durán, Marena Rein, Daniella Delgado et al.· Frontiers in Pharmacology· 0 citations
This work identifies a conserved gating crosstalk mechanism linking the activation gate to the width of the selectivity filter entrance, which regulates ion permeation rate by tuning ion occupancy at the selectivity filter.
Lyubin Hu, B. D. de Groot, Ruo-Xu Gu· Proceedings of the National...· 0 citations
This article shows that this plasticity is governed by a distal allosteric network that allows TPC2 to discriminate between agonists and generate specific lysosomal ion fluxes, and Mutant channels exhibit enhanced Ca²⁺ permeability and adopt a co-activated-like state.
Cryo-EM structures across all TRP subfamilies reveal how TRP channels coordinate Ca2+, how Ca2+ binding modulates pore opening or inactivation, and why some TRPs are highly Ca2+ selective while others are Ca2+ impermeable.
Bahar Bazeli, Laura Vangeel, Thomas Voets· Cold Spring Harbor Perspecti...· 0 citations
A detailed study of the properties and functions of Kv7 and GIRK potassium channels will provide a deeper understanding of the therapeutic potential of using their antagonists and agonists for the treatment of various neurological, including neuromuscular, diseases.
I. V. Kovyazina, A. Tsentsevitsky, A. M. Petrov· Biochemistry (Moscow) Supple...· 0 citations
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.