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Dear Colleagues,

This Special Issue follows the publication of the first edition of “State-of-the-Art Molecular Biology in Chile”.

Molecular biology has been fundamental to the study of different processes that occur in cell, tissue, and animal physiology. Indeed, this discipline has helped us understand how the interaction between proteins, nucleic acids, lipids, etc., accounts for numerous cellular processes. Furthermore, molecular biology has served to unveil several pathways that become dysfunctional during pathological settings, helping to develop several tools to improve cell and tissue function.

Chilean scientists have a long tradition of continuous contribution to the understanding of how cells/organisms work, and have used molecular biology as one valuable tool for this purpose. For this reason, the main aim of this Special Issue is to highlight recent advances in molecular and cell physiology performed by Chilean scientists, where the use of molecular biology has been instrumental. This call for articles will include genetics, cell biology/physiology, and molecular biology experimental approaches. Potential topics include, but are not limited to, the following:

Molecular biology in neurophysiology;
Molecular biology in physiology and cellular physiology;
Molecular biology in genetics;
Molecular biology in immunology;
Molecular biology in pharmacology.

Dr. Mauricio A. Retamal
Dr. Rodrigo Del Rio
Guest Editors

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Keywords

molecular biology
Chilean scientists
neurophysiology
physiology and cellular physiology
genetics
ecology
immunology
pharmacology

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21 pages, 3884 KiB

Open AccessArticle

Trapping Charge Mechanism in Hv1 Channels (CiHv1)

by Miguel Fernández, Juan J. Alvear-Arias, Emerson M. Carmona, Christian Carrillo, Antonio Pena-Pichicoi, Erick O. Hernandez-Ochoa, Alan Neely, Osvaldo Alvarez, Ramon Latorre, Jose A. Garate and Carlos Gonzalez

Int. J. Mol. Sci. 2024, 25(1), 426; https://doi.org/10.3390/ijms25010426 - 28 Dec 2023

Viewed by 637

Abstract

The majority of voltage-gated ion channels contain a defined voltage-sensing domain and a pore domain composed of highly conserved amino acid residues that confer electrical excitability via electromechanical coupling. In this sense, the voltage-gated proton channel (Hv1) is a unique protein in that voltage-sensing, proton permeation and pH-dependent modulation involve the same structural region. In fact, these processes synergistically work in concert, and it is difficult to separate them. To investigate the process of Hv1 voltage sensor trapping, we follow voltage-sensor movements directly by leveraging mutations that enable the measurement of Hv1 channel gating currents. We uncover that the process of voltage sensor displacement is due to two driving forces. The first reveals that mutations in the selectivity filter (D160) located in the S1 transmembrane interact with the voltage sensor. More hydrophobic amino acids increase the energy barrier for voltage sensor activation. On the other hand, the effect of positive charges near position 264 promotes the formation of salt bridges between the arginines of the voltage sensor domain, achieving a stable conformation over time. Our results suggest that the activation of the Hv1 voltage sensor is governed by electrostatic–hydrophobic interactions, and S4 arginines, N264 and selectivity filter (D160) are essential in the Ciona-Hv1 to understand the trapping of the voltage sensor. Full article

(This article belongs to the Special Issue State-of-the-Art Molecular Biology in Chile, 2nd Edition)

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