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Membranes
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Ion Channel in Lipid Environment
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Ion Channel in Lipid Environment

A special issue of Membranes (ISSN 2077-0375). This special issue belongs to the section "Biological Membrane Functions".

Deadline for manuscript submissions: closed (25 August 2022) | Viewed by 8033

Special Issue Editors

Dr. Lige Tonggu

E-Mail Website
Guest Editor
School of Medicine, University of Washington, Seattle, WA, USA
Interests: ion channel structure; cryo-EM; molecular basis of ion channel associated diseases and neurotoxins action
Dr. Yuan Gao

E-Mail Website
Guest Editor
Department of Cell Biology, Harvard Medical School and Howard Hughes Medical Institute, Boston, MA 02115, USA
Interests: TRP channel; cryo-EM; protein translocation; peroxisomal protein import

Special Issue Information

Dear Colleagues,

Ion channels are a major class of membrane proteins which are present in all cells. They are essential to many organisms’ physiological functions. In particular, ion channels constitute important drug targets for many diseases, including neurological and non-neurological disorders such as epilepsy, long QT syndromes and cystic fibrosis. Despite their central role in health and disease, they are notoriously difficult to study, especially in the native lipid environment. In recent years, with more advanced technology, we have seen a growing enthusiasm among researchers trying to tackle these challenges and start answering the question: How do ion channels work in the biological membrane?

To further promote this exciting field, we are pleased to invite you to contribute to the present Special Issue. It focuses on revealing recent developments in methods for the study of ion channels in lipid environments, and discussing structural and functional results in particular ion channels.

This Special Issue aims to focus on methods of ion channels reconstitution, as well as novel platforms for ion channel functional assay and structural determination. We also welcome papers related to the regulation of particular ion channels by membrane lipids and computational studies of ion channels in membranes.

In this Special Issue, original research articles and reviews are welcome. Research areas may include (but are not limited to) the following:

  • Methods for ion channel reconstitution;
  • Structural studies of ion channels in lipid environments (cryo-EM, NMR, X-ray crystallography);
  • Functional studies of ion channels in lipid environments;
  • Lipid regulation of ion channels;
  • Computational simulations of ion channels in membranes;
  • Computational designs of ion channels in membranes.

We look forward to publishing your outstanding work in this Special Issue.

Dr. Lige Tonggu
Dr. Yuan Gao
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Membranes is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • ion channels
  • lipid nanodiscs
  • polymer-encased nanodiscs
  • liposomes
  • ion channel functional assays
  • ion channel structural studies
  • molecular dynamic simulations

Published Papers (4 papers)

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Research

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13 pages, 2308 KiB  
Article
Structure of the Human BK Ion Channel in Lipid Environment
by Lige Tonggu and Liguo Wang
Membranes 2022, 12(8), 758; https://doi.org/10.3390/membranes12080758 - 31 Jul 2022
Cited by 8 | Viewed by 2461
Abstract
Voltage-gated and ligand-modulated ion channels play critical roles in excitable cells. To understand the interplay among voltage sensing, ligand binding, and channel opening, the structures of ion channels in various functional states and in lipid membrane environments need to be determined. Here, the [...] Read more.
Voltage-gated and ligand-modulated ion channels play critical roles in excitable cells. To understand the interplay among voltage sensing, ligand binding, and channel opening, the structures of ion channels in various functional states and in lipid membrane environments need to be determined. Here, the random spherically constrained (RSC) single-particle cryo-EM method was employed to study human large conductance voltage- and calcium-activated potassium (hBK or hSlo1) channels reconstituted into liposomes. The hBK structure was determined at 3.5 Å resolution in the absence of Ca2+. Instead of the common fourfold symmetry observed in ligand-modulated ion channels, a twofold symmetry was observed in hBK in liposomes. Compared with the structure of isolated hSlo1 Ca2+ sensing gating rings, two opposing subunits in hBK unfurled, resulting in a wider opening towards the transmembrane region of hBK. In the pore gate domain, two opposing subunits also moved downwards relative to the two other subunits. Full article
(This article belongs to the Special Issue Ion Channel in Lipid Environment)
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12 pages, 1557 KiB  
Article
Dynamic Distribution of ASIC1a Channels and Other Proteins within Cells Detected through Fractionation
by Libia Catalina Salinas Castellanos, Rodolfo Gabriel Gatto, Silvia Adriana Menchón, Matías Blaustein, Osvaldo Daniel Uchitel and Carina Weissmann
Membranes 2022, 12(4), 389; https://doi.org/10.3390/membranes12040389 - 31 Mar 2022
Cited by 1 | Viewed by 1699
Abstract
Proteins in eukaryotic cells reside in different cell compartments. Many studies require the specific localization of proteins and the detection of any dynamic changes in intracellular protein distribution. There are several methods available for this purpose that rely on the fractionation of the [...] Read more.
Proteins in eukaryotic cells reside in different cell compartments. Many studies require the specific localization of proteins and the detection of any dynamic changes in intracellular protein distribution. There are several methods available for this purpose that rely on the fractionation of the different cell compartments. Fractionation protocols have evolved since the first use of a centrifuge to isolate organelles. In this study, we described a simple method that involves the use of a tabletop centrifuge and different detergents to obtain cell fractions enriched in cytosolic (Cyt), plasma membrane (PM), membranous organelle (MO), and nuclear (Nu) proteins and identify the proteins in each fraction. This method serves to identify transmembrane proteins such as channel subunits as well as PM-embedded or weakly associated proteins. This protocol uses a minute amount of cell material and typical equipment present in laboratories, and it takes approximately 3 h. The process was validated using endogenous and exogenous proteins expressed in the HEK293T cell line that were targeted to each compartment. Using a specific stimulus as a trigger, we showed and quantified the shuttling of a protein channel (ASIC1a, acid sensing ion channel) from the MO fraction to the PM fraction and the shuttling of a kinase from a cytosolic location to a nuclear location. Full article
(This article belongs to the Special Issue Ion Channel in Lipid Environment)
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Review

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16 pages, 2643 KiB  
Review
Structural Pharmacology of Cation-Chloride Cotransporters
by Yongxiang Zhao and Erhu Cao
Membranes 2022, 12(12), 1206; https://doi.org/10.3390/membranes12121206 - 29 Nov 2022
Cited by 4 | Viewed by 2171
Abstract
Loop and thiazide diuretics have been cornerstones of clinical management of hypertension and fluid overload conditions for more than five decades. The hunt for their molecular targets led to the discovery of cation-chloride cotransporters (CCCs) that catalyze electroneutral movement of Cl− together [...] Read more.
Loop and thiazide diuretics have been cornerstones of clinical management of hypertension and fluid overload conditions for more than five decades. The hunt for their molecular targets led to the discovery of cation-chloride cotransporters (CCCs) that catalyze electroneutral movement of Cl− together with Na+ and/or K+. CCCs consist of two 1 Na+-1 K+-2 Cl− (NKCC1-2), one 1 Na+-1 Cl− (NCC), and four 1 K+-1 Cl− (KCC1-4) transporters in human. CCCs are fundamental in trans-epithelia ion secretion and absorption, homeostasis of intracellular Cl− concentration and cell volume, and regulation of neuronal excitability. Malfunction of NKCC2 and NCC leads to abnormal salt and water retention in the kidney and, consequently, imbalance in electrolytes and blood pressure. Mutations in KCC2 and KCC3 are associated with brain disorders due to impairments in regulation of excitability and possibly cell volume of neurons. A recent surge of structures of CCCs have defined their dimeric architecture, their ion binding sites, their conformational changes associated with ion translocation, and the mechanisms of action of loop diuretics and small molecule inhibitors. These breakthroughs now set the stage to expand CCC pharmacology beyond loop and thiazide diuretics, developing the next generation of diuretics with improved potency and specificity. Beyond drugging renal-specific CCCs, brain-penetrable therapeutics are sorely needed to target CCCs in the nervous system for the treatment of neurological disorders and psychiatric conditions. Full article
(This article belongs to the Special Issue Ion Channel in Lipid Environment)
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8 pages, 562 KiB  
Review
Novel Perspective of Cardiovascular Diseases: Volume-Regulatory Anion Channels in the Cell Membrane
by Liming Hou, Yan Liu, Chao Sun, Rong Xu, Guihua Cao and Xiaoming Wang
Membranes 2022, 12(7), 644; https://doi.org/10.3390/membranes12070644 - 23 Jun 2022
Cited by 1 | Viewed by 1214
Abstract
Cardiovascular diseases (CVDs) are the leading cause of morbidity and mortality worldwide. Although there are established mechanisms and preventions for CVDs, they are not totally elucidative and effective. Emerging evidence suggests that the dysregulation of ion channels in the cell membranes underpins the [...] Read more.
Cardiovascular diseases (CVDs) are the leading cause of morbidity and mortality worldwide. Although there are established mechanisms and preventions for CVDs, they are not totally elucidative and effective. Emerging evidence suggests that the dysregulation of ion channels in the cell membranes underpins the dysfunction of the cardiovascular system. To date, a variety of cation channels have been widely recognized as important targets for the treatment of CVDs. As a critical component of the anion channels, the volume-regulated anion channel (VRAC) is involved in a series of cell functions by the volume regulation and maintenance of membrane homeostasis. It has been confirmed to play crucial roles in cell action potential generation, cell proliferation, differentiation and apoptosis, and the VRAC appears to be a major participant in metabolic processes during CVDs. This review summarizes the current evidence and progress concerning the VRAC, to determine the future directions and challenges for CVDs for both preventive and therapeutic purposes. Full article
(This article belongs to the Special Issue Ion Channel in Lipid Environment)
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