Identification and characterization of the zebrafish ClC-2 chloride channel orthologs

ClC-2 is a Cl − channel that belongs to the CLC family of chloride channel/transport proteins. ClC-2 molecular role is not clear, and Clcn2 knockout mice develop blindness, sterility, and leukodystrophy by unknown reasons. ClC-2 is associated in the brain with the adhesion molecule GlialCAM, which i...

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Veröffentlicht in:Pflügers Archiv 2015-08, Vol.467 (8), p.1769-1781
Hauptverfasser: Pérez-Rius, Carla, Gaitán-Peñas, Héctor, Estévez, Raúl, Barrallo-Gimeno, Alejandro
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creator Pérez-Rius, Carla
Gaitán-Peñas, Héctor
Estévez, Raúl
Barrallo-Gimeno, Alejandro
description ClC-2 is a Cl − channel that belongs to the CLC family of chloride channel/transport proteins. ClC-2 molecular role is not clear, and Clcn2 knockout mice develop blindness, sterility, and leukodystrophy by unknown reasons. ClC-2 is associated in the brain with the adhesion molecule GlialCAM, which is defective in a type of leukodystrophy, involving ClC-2 in the homeostasis of myelin. To get more insight into the functions of ClC-2, we have identified in this work the three ClC-2 orthologs in zebrafish. clcn2a and clcn2b resulted from the teleost-specific whole genome duplication, while clcn2c arose from a gene duplication from clcn2b . The expression patterns in adult tissues and embryos of zebrafish clcn2 paralogs support their subfunctionalization after the duplications, with clcn2a being enriched in excitable tissues and clcn2c in ionocytes. All three zebrafish clc-2 proteins interact with human GLIALCAM, that is able to target them to cell junctions, as it does with mammalian ClC-2. We could detect clc-2a and clc-2b inward rectified chloride currents with different voltage-dependence and kinetics in Xenopus oocytes, while clc-2c remained inactive. Interestingly, GlialCAM proteins did not modify clc-2b inward rectification. Then, our work extends the repertoire of ClC-2 proteins and provides new tools for structure-function and physiology studies.
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We could detect clc-2a and clc-2b inward rectified chloride currents with different voltage-dependence and kinetics in Xenopus oocytes, while clc-2c remained inactive. Interestingly, GlialCAM proteins did not modify clc-2b inward rectification. 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subjects Amino Acid Sequence
Animals
Biomedical and Life Sciences
Biomedicine
Canals de clorur
Cell Biology
Chloride channels
Chloride Channels - chemistry
Chloride Channels - genetics
Chloride Channels - metabolism
Chlorides - metabolism
Danio rerio
Databases, Genetic
Gene Expression Regulation, Developmental
Human Physiology
Ion Channels
Kinetics
Membrane Potentials
Metabolisme de proteïnes
Molecular Medicine
Molecular Sequence Data
Neurosciences
Nucleotide sequence
Oocytes
Peix zebra
Phylogeny
Protein Binding
Protein metabolism
Protein Transport
Proteins - metabolism
Receptors
Receptors and Transporters
RNA, Messenger - metabolism
Seqüència de nucleòtids
Xenopus
Zebra danio
Zebrafish - embryology
Zebrafish - genetics
Zebrafish - metabolism
Zebrafish Proteins - chemistry
Zebrafish Proteins - genetics
Zebrafish Proteins - metabolism
title Identification and characterization of the zebrafish ClC-2 chloride channel orthologs
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