Proton channels in molluscs: A new bivalvian‐specific minimal H V 4 channel
Recently, three proton channels (H V ) have been identified and characterized in Aplysia californica (AcH V 1‐3). Focusing on AcH V 1 and AcH V 2, analysis of Transcriptome Shotgun Assembly and genomic databases of 91 molluscs identified H V homologous channels in other molluscs: channels homologous...
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crwiley:10.1111/febs.16751 2024-03-31T07:52:24+00:00 Proton channels in molluscs: A new bivalvian‐specific minimal H V 4 channel Chaves, Gustavo Jardin, Christophe Franzen, Arne Mahorivska, Iryna Musset, Boris Derst, Christian 2023 http://dx.doi.org/10.1111/febs.16751 https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.16751 https://onlinelibrary.wiley.com/doi/full-xml/10.1111/febs.16751 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.16751 en eng Wiley http://creativecommons.org/licenses/by-nc/4.0/ The FEBS Journal volume 290, issue 13, page 3436-3447 ISSN 1742-464X 1742-4658 Cell Biology Molecular Biology Biochemistry journal-article 2023 crwiley https://doi.org/10.1111/febs.16751 2024-03-04T13:03:05Z Recently, three proton channels (H V ) have been identified and characterized in Aplysia californica (AcH V 1‐3). Focusing on AcH V 1 and AcH V 2, analysis of Transcriptome Shotgun Assembly and genomic databases of 91 molluscs identified H V homologous channels in other molluscs: channels homologous to AcH V 1 and to AcH V 2 were found in 90 species (56 full‐length sequences) and in 33 species (18 full‐length sequences), respectively. Here, we report the discovery of a fourth distinct proton channel family, H V 4. This new family has high homology to AcH V 1 and AcH V 2 and was identified only in bivalvian molluscs (13 species, 12 full‐length sequences). Typically, these channels possess an extracellular S1–S2 loop of intermediate size (~ 20 amino acids) compared to the shorter loops of molluscan H V 1 channels (~ 13 amino acids) and the much larger loops of molluscan H V 2 channels (> 65 amino acids). The characteristic voltage‐sensor motif in S4 possesses only two arginine residues with the common third arginine being replaced by a lysine. Moreover, H V 4 channels are much smaller with only around 200 amino acids in total length. The smallest functional channel found so far in nature (189 amino acids) is expressed in the pacific oyster Crassostrea gigas (CgH V 4) and might be considered an archetypical minimal proton channel. Functional expression and electrophysiological characterization demonstrated that CgH V 4 shares distinctive hallmarks of other investigated proton channels as high proton selectivity, slow activation, and pH‐ and voltage‐regulated gating. This work is the first description of a H V 4 type channel, adding a new member to the recently expanded family of proton channels. Article in Journal/Newspaper Crassostrea gigas Pacific oyster Wiley Online Library Pacific The FEBS Journal 290 13 3436 3447 |
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Open Polar |
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Wiley Online Library |
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crwiley |
language |
English |
topic |
Cell Biology Molecular Biology Biochemistry |
spellingShingle |
Cell Biology Molecular Biology Biochemistry Chaves, Gustavo Jardin, Christophe Franzen, Arne Mahorivska, Iryna Musset, Boris Derst, Christian Proton channels in molluscs: A new bivalvian‐specific minimal H V 4 channel |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
Recently, three proton channels (H V ) have been identified and characterized in Aplysia californica (AcH V 1‐3). Focusing on AcH V 1 and AcH V 2, analysis of Transcriptome Shotgun Assembly and genomic databases of 91 molluscs identified H V homologous channels in other molluscs: channels homologous to AcH V 1 and to AcH V 2 were found in 90 species (56 full‐length sequences) and in 33 species (18 full‐length sequences), respectively. Here, we report the discovery of a fourth distinct proton channel family, H V 4. This new family has high homology to AcH V 1 and AcH V 2 and was identified only in bivalvian molluscs (13 species, 12 full‐length sequences). Typically, these channels possess an extracellular S1–S2 loop of intermediate size (~ 20 amino acids) compared to the shorter loops of molluscan H V 1 channels (~ 13 amino acids) and the much larger loops of molluscan H V 2 channels (> 65 amino acids). The characteristic voltage‐sensor motif in S4 possesses only two arginine residues with the common third arginine being replaced by a lysine. Moreover, H V 4 channels are much smaller with only around 200 amino acids in total length. The smallest functional channel found so far in nature (189 amino acids) is expressed in the pacific oyster Crassostrea gigas (CgH V 4) and might be considered an archetypical minimal proton channel. Functional expression and electrophysiological characterization demonstrated that CgH V 4 shares distinctive hallmarks of other investigated proton channels as high proton selectivity, slow activation, and pH‐ and voltage‐regulated gating. This work is the first description of a H V 4 type channel, adding a new member to the recently expanded family of proton channels. |
format |
Article in Journal/Newspaper |
author |
Chaves, Gustavo Jardin, Christophe Franzen, Arne Mahorivska, Iryna Musset, Boris Derst, Christian |
author_facet |
Chaves, Gustavo Jardin, Christophe Franzen, Arne Mahorivska, Iryna Musset, Boris Derst, Christian |
author_sort |
Chaves, Gustavo |
title |
Proton channels in molluscs: A new bivalvian‐specific minimal H V 4 channel |
title_short |
Proton channels in molluscs: A new bivalvian‐specific minimal H V 4 channel |
title_full |
Proton channels in molluscs: A new bivalvian‐specific minimal H V 4 channel |
title_fullStr |
Proton channels in molluscs: A new bivalvian‐specific minimal H V 4 channel |
title_full_unstemmed |
Proton channels in molluscs: A new bivalvian‐specific minimal H V 4 channel |
title_sort |
proton channels in molluscs: a new bivalvian‐specific minimal h v 4 channel |
publisher |
Wiley |
publishDate |
2023 |
url |
http://dx.doi.org/10.1111/febs.16751 https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.16751 https://onlinelibrary.wiley.com/doi/full-xml/10.1111/febs.16751 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.16751 |
geographic |
Pacific |
geographic_facet |
Pacific |
genre |
Crassostrea gigas Pacific oyster |
genre_facet |
Crassostrea gigas Pacific oyster |
op_source |
The FEBS Journal volume 290, issue 13, page 3436-3447 ISSN 1742-464X 1742-4658 |
op_rights |
http://creativecommons.org/licenses/by-nc/4.0/ |
op_doi |
https://doi.org/10.1111/febs.16751 |
container_title |
The FEBS Journal |
container_volume |
290 |
container_issue |
13 |
container_start_page |
3436 |
op_container_end_page |
3447 |
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1795031512149655552 |