Dr. Wendy González

Director of the Center for Bioinformatics, Simulations and Modelling (CBSM) University of Talca, Talca 3460000, Chile

Dr. Wendy González

Director of the Center for Bioinformatics, Simulations and Modelling (CBSM) University of Talca, Talca 3460000, Chile

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Academic Career Length

23Years (2004-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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27 December 2010 in Proceedings of the National Academy of Sciences

Journal Article

Potassium (K ⁺ ) gradients serve as a mobile energy source in plant vascular tissues

Pawel Gajdanowicz

Erwan Michard

Michael Sandmann

Marcio Rocha

Luiz Gustavo Guedes Corrêa

Ingo Dreyer

The essential mineral nutrient potassium (K ⁺ ) is the most important inorganic cation for plants and is recognized as a limiting factor for crop yield and quality. Nonetheless, it is only partially understood how K ⁺ contributes to plant productivity. K ⁺ is used as a major active solute to maintain turgor and to drive irreversible and reversible changes in cell volume. K ⁺ also plays an important role in numerous metabolic processes, for example, by serving as an essential cofactor of enzymes. Here, we provide evidence for an additional, previously unrecognized role of K ⁺ in plant growth. By combining diverse experimental approaches with computational cell simulation, we show that K ⁺ circulating in the phloem serves as a decentralized energy storage that can be used to overcome local energy limitations. Posttranslational modification of the phloem-expressed Arabidopsis K ⁺ channel AKT2 taps this “potassium battery,” which then efficiently assists the plasma membrane H ⁺ -ATPase in energizing the transmembrane phloem (re)loading processes.

22 February 2019 in Science

Journal Article

A pharmacological master key mechanism that unlocks the selectivity filter gate in K ⁺ channels

Marcus Schewe

Han Sun

ÜM

Ümit Mert

Alexandra Mackenzie

Ashley C. W. Pike

Thomas Baukrowitz

+16

A key to potassium channel activation: Using drugs to activate potassium channels has the potential to treat conditions like epilepsy, heart arrhythmias, and pain. Schewe et al. report a class of negatively charged activators (NCAs) with a defined pharmacore that use a similar mechanism to activate many types of potassium channels. X-ray crystallography, functional analysis, and molecular dynamics simulations showed that the NCAs bind below the selectivity filter to open the filter gate and activate the channels. Targeting this NCA site might be exploited in rational drug design. Science , this issue p. 875

1 September 2010 in Journal of Biological Chemistry

Journal Article

A Minimal Cysteine Motif Required to Activate the SKOR K+ Channel of Arabidopsis by the Reactive Oxygen Species H2O2*

Pawel Gajdanowicz

Adrian Hills

Reactive oxygen species (ROS) are essential for development and stress signaling in plants. They contribute to plant defense against pathogens, regulate stomatal transpiration, and influence nutrient uptake and partitioning. Although both Ca²⁺ and K⁺ channels of plants are known to be affected, virtually nothing is known of the targets for ROS at a molecular level. Here we report that a single cysteine (Cys) residue within the Kv-like SKOR K⁺ channel of Arabidopsis thaliana is essential for channel sensitivity to the ROS H₂O₂. We show that H₂O₂ rapidly enhanced current amplitude and activation kinetics of heterologously expressed SKOR, and the effects were reversed by the reducing agent dithiothreitol (DTT). Both H₂O₂ and DTT were active at the outer face of the membrane and current enhancement was strongly dependent on membrane depolarization, consistent with a H₂O₂-sensitive site on the SKOR protein that is exposed to the outside when the channel is in the open conformation. Cys substitutions identified a single residue, Cys¹⁶⁸ located within the S3 α-helix of the voltage sensor complex, to be essential for sensitivity to H₂O₂. The same Cys residue was a primary determinant for current block by covalent Cys S-methioylation with aqueous methanethiosulfonates. These, and additional data identify Cys¹⁶⁸ as a critical target for H₂O₂, and implicate ROS-mediated control of the K⁺ channel in regulating mineral nutrient partitioning within the plant.

23 April 2015 in Human Mutation

Journal Article

Mutation Update of theCLCN5Gene Responsible for Dent Disease 1

Lamisse Mansour-Hendili

Anne Blanchard

Nelly Le Pottier

Isabelle Roncelin

Stéphane Lourdel

Rosa Vargas-Poussou

+62

Dent disease is a rare X‐linked tubulopathy characterized by low molecular weight proteinuria, hypercalciuria, nephrocalcinosis and/or nephrolithiasis, progressive renal failure, and variable manifestations of other proximal tubule dysfunctions. It often progresses over a few decades to chronic renal insufficiency, and therefore molecular characterization is important to allow appropriate genetic counseling. Two genetic subtypes have been described to date: Dent disease 1 is caused by mutations of the CLCN5 gene, coding for the chloride/proton exchanger ClC‐5; and Dent disease 2 by mutations of the OCRL gene, coding for the inositol polyphosphate 5‐phosphatase OCRL‐1. Herein, we review previously reported mutations (n = 192) and their associated phenotype in 377 male patients with Dent disease 1 and describe phenotype and novel (n = 42) and recurrent mutations (n = 24) in a large cohort of 117 Dent disease 1 patients belonging to 90 families. The novel missense and in‐frame mutations described were mapped onto a three‐dimensional homology model of the ClC‐5 protein. This analysis suggests that these mutations affect the dimerization process, helix stability, or transport. The phenotype of our cohort patients supports and extends the phenotype that has been reported in smaller studies.

14 February 2021 in International Journal of Molecular Sciences

Journal Article

Plant HKT Channels: An Updated View on Structure, Function and Gene Regulation

Janin Riedelsberger

Julia Miller

Braulio Valdebenito Maturana

Miguel A. Piñeros

Wendy González

Ingo Dreyer

HKT channels are a plant protein family involved in sodium (Na⁺) and potassium (K⁺) uptake and Na⁺-K⁺ homeostasis. Some HKTs underlie salt tolerance responses in plants, while others provide a mechanism to cope with short-term K⁺ shortage by allowing increased Na⁺ uptake under K⁺ starvation conditions. HKT channels present a functionally versatile family divided into two classes, mainly based on a sequence polymorphism found in the sequences underlying the selectivity filter of the first pore loop. Physiologically, most class I members function as sodium uniporters, and class II members as Na⁺/K⁺ symporters. Nevertheless, even within these two classes, there is a high functional diversity that, to date, cannot be explained at the molecular level. The high complexity is also reflected at the regulatory level. HKT expression is modulated at the level of transcription, translation, and functionality of the protein. Here, we summarize and discuss the structure and conservation of the HKT channel family from algae to angiosperms. We also outline the latest findings on gene expression and the regulation of HKT channels.

9 January 2007 in Proceedings of the National Academy of Sciences

Journal Article

Neutralization of a single arginine residue gates open a two-pore domain, alkali-activated K ⁺ channel

María Isabel Niemeyer

Fernando Gonzalez-Nilo

Leandro Zúñiga

Wendy González

L. Pablo Cid

Francisco V. Sepúlveda

Potassium channels share a common selectivity filter that determines the conduction characteristics of the pore. Diversity in K ⁺ channels is given by how they are gated open. TASK-2, TALK-1, and TALK-2 are two-pore region (2P) KCNK K ⁺ channels gated open by extracellular alkalinization. We have explored the mechanism for this alkalinization-dependent gating using molecular simulation and site-directed mutagenesis followed by functional assay. We show that the side chain of a single arginine residue (R224) near the pore senses pH in TASK-2 with an unusual pK _a of 8.0, a shift likely due to its hydrophobic environment. R224 would block the channel through an electrostatic effect on the pore, a situation relieved by its deprotonation by alkalinization. A lysine residue in TALK-2 fulfills the same role but with a largely unchanged pK _a , which correlates with an environment that stabilizes its positive charge. In addition to suggesting unified alkaline pH-gating mechanisms within the TALK subfamily of channels, our results illustrate in a physiological context the principle that hydrophobic environment can drastically modulate the pK _a of charged amino acids within a protein.

About Me

W.G. studied Biology at the University of Havana, Cuba (1998-2003). During the last two years of her undergraduate studies, W.G. was trained as a specialist in Bioinformatics at CIGB in Havana, Cuba. In 2004, Wendy moved to Chile and worked as research assistant at CECs where she met her scientific passion, the ion channels, in the group of Ramón Latorre. Later, she continued with doctoral studies (2005-2010) in the group of Prof. Danilo González studying potassium channels in plants with a structural point of view at Universidad de Talca. Wendy obtained her Ph.D. funded by ANID. Afterward, she won her first grant (Fondecyt de Iniciación) to study K2P channels in plants and animals. Simultaneously, she received expert training in plant biophysics as a postdoctoral researcher in the laboratory of Prof. Ingo Dreyer at the University of Potsdam, Germany. In 2012, she became director of the Center for Bioinformatics, Simulations and Modeling at Universidad de Talca and assistant professor. In 2014, she obtained her second grant (Fondecyt Regular) and became Associate Professor at Universidad de Talca. In 2019, she obtained her third grant (Fondecyt Regular) and became full professor in 2021. Since 2017, Wendy has been a researcher of the Millennium Nucleus of Ion Channels-Associated Diseases (MiNICAD). Currently, she is studying through her third Fondecyt grant the “Structural insights into the mechanism of multi-channel blockers of atrial ion channels”.

Dr. Wendy González

Dr. Wendy González

Research Focus & Metrics

Academic Career Length

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Representative Publications

About Me