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Protein Structural Modeling and Transport Thermodynamics Reveal That Plant Cation-Chloride Cotransporters Mediate Potassium-Chloride Symport.
Int J Mol Sci
December 2024
School of Agriculture, Food and Wine, Waite Research Institute, Faculty of Sciences, Engineering and Technology, University of Adelaide, Waite Campus Precinct, Glen Osmond, Adelaide, SA 5064, Australia.
Plant cation-chloride cotransporters (CCCs) are proposed to be Na-K-2Cl transporting membrane proteins, although evolutionarily, they associate more closely with K-Cl cotransporters (KCCs). Here, we investigated grapevine ( L.) VvCCC using 3D protein modeling, bioinformatics, and electrophysiology with a heterologously expressed protein.
View Article and Find Full Text PDFStructure-Function Relationship of a Novel MTX-like Peptide (MTX1) Isolated and Characterized from the Venom of the Scorpion .
Int J Mol Sci
September 2024
Laboratory of Venoms and Therapeutic Biomolecules, Pasteur Institute of Tunis, University of Tunis El Manar, 13 Place Pasteur, BP74, Tunis 1002, Tunisia.
Maurotoxin (MTX) is a 34-residue peptide from venom. It is reticulated by four disulfide bridges with a unique arrangement compared to other scorpion toxins that target potassium (K) channels. Structure-activity relationship studies have not been well performed for this toxin family.
View Article and Find Full Text PDFThe Janus (dual) model of immunoglobulin isotype evolution: Conservation and plasticity are the defining paradigms.
Immunol Rev
November 2024
Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
The study of antibodies in jawed vertebrates (gnathostomes) provides every immunologist with a bird's eye view of how human immunoglobulins (Igs) came into existence and subsequently evolved into their present forms. It is a fascinating Darwinian history of conservation on the one hand and flexibility on the other, exemplified by the Ig heavy chain (H) isotypes IgM and IgD/W, respectively. The cartilaginous fish (e.
View Article and Find Full Text PDFCharacterization of human aquaporin ion channels in a yeast expression system as a tool for novel ion channel discovery.
Biosci Rep
August 2024
School of Biomedicine, Faculty of Health and Medical Sciences, and the Institute for Photonics and Advanced Sensing, University of Adelaide, Adelaide, SA 5005, Australia.
Aquaporin (AQP) channels found in all domains of life are transmembrane proteins which mediate passive transport of water, glycerol, signaling molecules, metabolites, and charged solutes. Discovery of new classes of ion-conducting AQP channels has been slow, likely reflecting time- and labor-intensive methods required for traditional electrophysiology. Work here defines a sensitive mass-throughput system for detecting AQP ion channels, identified by rescue of cell growth in the K+-transport-defective yeast strain CY162 following genetic complementation with heterologously expressed cation-permeable channels, using the well characterized human AQP1 channel for proof of concept.
View Article and Find Full Text PDFCharacterization of ClC-1 chloride channels in zebrafish: a new model to study myotonia.
J Physiol
August 2024
Physiology Unit, Department of Physiological Sciences, School of Medicine and Health Sciences, Institute of Neurosciences, University of Barcelona-IDIBELL, Barcelona, Spain.
The function of the chloride channel ClC-1 is crucial for the control of muscle excitability. Thus, reduction of ClC-1 functions by CLCN1 mutations leads to myotonia congenita. Many different animal models have contributed to understanding the myotonia pathophysiology.
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