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C-terminus-independent multimerization of Hv1 proton channels.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: C-terminus-independent multimerization of Hv1 proton channels.
Συγγραφείς: Rosa V; Departamento de Fisiología, Facultad de Medicina, UNAM, Mexico City, Mexico., Rangel-Yescas GE; Departamento de Fisiología, Facultad de Medicina, UNAM, Mexico City, Mexico., Flores-Herrera O; Departamento de Bioquímica, Facultad de Medicina, UNAM, Mexico City, Mexico., Esparza-Perusquia M; Departamento de Bioquímica, Facultad de Medicina, UNAM, Mexico City, Mexico., Cristóbal-Mondragón GR; Departamento de Fisiología, Facultad de Medicina, UNAM, Mexico City, Mexico., Ramsey IS; Department of Physiology and Biophysics, Virginia Commonwealth University, Richmond, Virginia, USA., Rosenbaum T; Departamento de Neurociencia Cognitiva, Instituto de Fisiología Celular, UNAM, Mexico City, Mexico., Islas LD; Departamento de Fisiología, Facultad de Medicina, UNAM, Mexico City, Mexico. Electronic address: leon.islas@gmail.com.
Πηγή: The Journal of biological chemistry [J Biol Chem] 2026 Sep; Vol. 302 (9), pp. 113387. Date of Electronic Publication: 2026 Aug 04.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
Imprint Name(s): Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
Ιατρικοί όροι (MeSH): Ion Channels*/chemistry , Ion Channels*/metabolism , Ion Channels*/genetics , Protein Multimerization*, Animals ; Humans ; Protein Domains ; Protons
Περίληψη: The voltage-gated proton channel Hv1, assembles as a dimer when expressed in heterologous systems, likely reflecting its stoichiometry in native membranes. It is known that the dimeric interaction is mediated at least by specific transmembrane domain amino acid interactions and a coiled-coil interaction mediated by the intracellular C-terminus helices. Deletion of this last interaction (ΔC) has been thought to lead to disruption of dimers and production of monomeric channels, which remain functional as proton channels, albeit with different biophysical properties. Here, we present evidence that apart from activation kinetics, other biophysical properties of the ΔC channels are different to those of the WT, dimeric channels, and that the ΔC channels are still capable of efficiently forming dimers and maybe even reaching higher stoichiometry. Our results suggest that the C-terminal-mediated interactions might help to ensure formation of dimers in full-length channels but are not necessary for their assembly.
(Copyright © 2026 The Authors. Published by Elsevier Inc. All rights reserved.)
Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
Contributed Indexing: Keywords: Voltage-gated proton channels; activation; channel gating; protein dimerization
Substance Nomenclature: 0 (Ion Channels)
0 (HVCN1 protein, human)
0 (Protons)
Entry Date(s): Date Created: 20260804 Date Completed: 20260922 Latest Revision: 20260922
Update Code: 20260923
PubMed Central ID: PMC13546843
DOI: 10.1016/j.jbc.2026.113387
PMID: 42551827
Βάση Δεδομένων: MEDLINE
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  Data: C-terminus-independent multimerization of Hv1 proton channels.
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  Data: <searchLink fieldCode="AU" term="%22Rosa+V%22">Rosa V</searchLink>; Departamento de Fisiología, Facultad de Medicina, UNAM, Mexico City, Mexico.<br /><searchLink fieldCode="AU" term="%22Rangel-Yescas+GE%22">Rangel-Yescas GE</searchLink>; Departamento de Fisiología, Facultad de Medicina, UNAM, Mexico City, Mexico.<br /><searchLink fieldCode="AU" term="%22Flores-Herrera+O%22">Flores-Herrera O</searchLink>; Departamento de Bioquímica, Facultad de Medicina, UNAM, Mexico City, Mexico.<br /><searchLink fieldCode="AU" term="%22Esparza-Perusquia+M%22">Esparza-Perusquia M</searchLink>; Departamento de Bioquímica, Facultad de Medicina, UNAM, Mexico City, Mexico.<br /><searchLink fieldCode="AU" term="%22Cristóbal-Mondragón+GR%22">Cristóbal-Mondragón GR</searchLink>; Departamento de Fisiología, Facultad de Medicina, UNAM, Mexico City, Mexico.<br /><searchLink fieldCode="AU" term="%22Ramsey+IS%22">Ramsey IS</searchLink>; Department of Physiology and Biophysics, Virginia Commonwealth University, Richmond, Virginia, USA.<br /><searchLink fieldCode="AU" term="%22Rosenbaum+T%22">Rosenbaum T</searchLink>; Departamento de Neurociencia Cognitiva, Instituto de Fisiología Celular, UNAM, Mexico City, Mexico.<br /><searchLink fieldCode="AU" term="%22Islas+LD%22">Islas LD</searchLink>; Departamento de Fisiología, Facultad de Medicina, UNAM, Mexico City, Mexico. Electronic address: leon.islas@gmail.com.
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  Data: <searchLink fieldCode="JN" term="%222985121R%22">The Journal of biological chemistry</searchLink> [J Biol Chem] 2026 Sep; Vol. 302 (9), pp. 113387. <i>Date of Electronic Publication: </i>2026 Aug 04.
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  Data: The voltage-gated proton channel Hv1, assembles as a dimer when expressed in heterologous systems, likely reflecting its stoichiometry in native membranes. It is known that the dimeric interaction is mediated at least by specific transmembrane domain amino acid interactions and a coiled-coil interaction mediated by the intracellular C-terminus helices. Deletion of this last interaction (ΔC) has been thought to lead to disruption of dimers and production of monomeric channels, which remain functional as proton channels, albeit with different biophysical properties. Here, we present evidence that apart from activation kinetics, other biophysical properties of the ΔC channels are different to those of the WT, dimeric channels, and that the ΔC channels are still capable of efficiently forming dimers and maybe even reaching higher stoichiometry. Our results suggest that the C-terminal-mediated interactions might help to ensure formation of dimers in full-length channels but are not necessary for their assembly.<br /> (Copyright © 2026 The Authors. Published by Elsevier Inc. All rights reserved.)
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  Data: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
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