Electrophysiological recordings and a liposome-based assay showing the absence of chloride and proton conduction in TTYH proteins
Data files
Jul 27, 2021 version files 656.85 KB
Aug 13, 2021 version files 724.61 MB
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Electrophysiological_recordings_and_a_liposome-based_assay_showing_the_absence_of_chloride_and_proton_conduction_in_TTYH_proteins_Readme.txt
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Electrophysiological_recordings_showing_the_absence_of_chloride_and_proton_conduction_in_TTYH_proteins.zip
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TTYH_absence_of_chloride_conduction.xlsx
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TTYH_absence_of_proton_conduction.xlsx
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Aug 16, 2021 version files 723.54 MB
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Electrophysiological_recordings_and_a_liposome-based_assay_showing_the_absence_of_chloride_and_proton_conduction_in_TTYH_proteins_Readme.txt
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Electrophysiological_recordings_showing_the_absence_of_chloride_and_proton_conduction_in_TTYH_proteins.zip
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TTYH_absence_of_chloride_conduction.xlsx
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TTYH_absence_of_proton_conduction.xlsx
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Aug 27, 2021 version files 723.54 MB
Abstract
The Tweety homologues (TTYHs) are members of a conserved family of eukaryotic membrane proteins that are abundant in the brain. The three human paralogs were assigned to function as anion channels that are either activated by Ca2+ or cell swelling. To uncover their unknown architecture and its relationship to function, we have determined the structures of human TTYH1–3 by cryo-electron microscopy. All structures display equivalent features of a dimeric membrane protein that contains five transmembrane segments and an extended extracellular domain. As none of the proteins shows features reminiscent of an anion channel, we revisited functional experiments and did not find any indication of ion conduction. Instead, we find density in an extended hydrophobic pocket contained in the extracellular domain that emerges from the lipid bilayer, which suggests a role of TTYH proteins in the interaction with lipid-like compounds residing in the membrane.