Academic Journal
C-terminus-independent multimerization of Hv1 proton channels.
| Τίτλος: | C-terminus-independent multimerization of Hv1 proton channels. |
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| 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 |
| ISSN: | 1083-351X |
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| DOI: | 10.1016/j.jbc.2026.113387 |