Recent advances on the structure and the function relationships of the TRPV4 ion channel
The members of the superfamily of Transient Receptor Potential (TRP) ion channels are physiologically important molecules that have been studied for many years and are still being intensively researched. Among the vanilloid TRP subfamily, the TRPV4 ion channel is an interesting protein due to its in...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2024-12-01
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| Series: | Channels |
| Subjects: | |
| Online Access: | https://www.tandfonline.com/doi/10.1080/19336950.2024.2313323 |
| _version_ | 1826945171061735424 |
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| author | Raúl Sánchez-Hernández Miguel Benítez-Angeles Ana M. Hernández-Vega Tamara Rosenbaum |
| author_facet | Raúl Sánchez-Hernández Miguel Benítez-Angeles Ana M. Hernández-Vega Tamara Rosenbaum |
| author_sort | Raúl Sánchez-Hernández |
| collection | DOAJ |
| description | The members of the superfamily of Transient Receptor Potential (TRP) ion channels are physiologically important molecules that have been studied for many years and are still being intensively researched. Among the vanilloid TRP subfamily, the TRPV4 ion channel is an interesting protein due to its involvement in several essential physiological processes and in the development of various diseases. As in other proteins, changes in its function that lead to the development of pathological states, have been closely associated with modification of its regulation by different molecules, but also by the appearance of mutations which affect the structure and gating of the channel. In the last few years, some structures for the TRPV4 channel have been solved. Due to the importance of this protein in physiology, here we discuss the recent progress in determining the structure of the TRPV4 channel, which has been achieved in three species of animals (Xenopus tropicalis, Mus musculus, and Homo sapiens), highlighting conserved features as well as key differences among them and emphasizing the binding sites for some ligands that play crucial roles in its regulation. |
| first_indexed | 2024-03-08T00:53:21Z |
| format | Article |
| id | doaj.art-e44d19c2f44647f1b0878a2f23c29dde |
| institution | Directory Open Access Journal |
| issn | 1933-6950 1933-6969 |
| language | English |
| last_indexed | 2025-02-17T20:50:37Z |
| publishDate | 2024-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Channels |
| spelling | doaj.art-e44d19c2f44647f1b0878a2f23c29dde2024-12-09T07:27:27ZengTaylor & Francis GroupChannels1933-69501933-69692024-12-0118110.1080/19336950.2024.2313323Recent advances on the structure and the function relationships of the TRPV4 ion channelRaúl Sánchez-Hernández0Miguel Benítez-Angeles1Ana M. Hernández-Vega2Tamara Rosenbaum3Departamento de Neurociencia Cognitiva, División Neurociencias, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico, MexicoDepartamento de Neurociencia Cognitiva, División Neurociencias, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico, MexicoDepartamento de Neurociencia Cognitiva, División Neurociencias, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico, MexicoDepartamento de Neurociencia Cognitiva, División Neurociencias, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico, MexicoThe members of the superfamily of Transient Receptor Potential (TRP) ion channels are physiologically important molecules that have been studied for many years and are still being intensively researched. Among the vanilloid TRP subfamily, the TRPV4 ion channel is an interesting protein due to its involvement in several essential physiological processes and in the development of various diseases. As in other proteins, changes in its function that lead to the development of pathological states, have been closely associated with modification of its regulation by different molecules, but also by the appearance of mutations which affect the structure and gating of the channel. In the last few years, some structures for the TRPV4 channel have been solved. Due to the importance of this protein in physiology, here we discuss the recent progress in determining the structure of the TRPV4 channel, which has been achieved in three species of animals (Xenopus tropicalis, Mus musculus, and Homo sapiens), highlighting conserved features as well as key differences among them and emphasizing the binding sites for some ligands that play crucial roles in its regulation.https://www.tandfonline.com/doi/10.1080/19336950.2024.2313323Ion channelTRPV4structureCryo-EM4α-PDDHC-067047 |
| spellingShingle | Raúl Sánchez-Hernández Miguel Benítez-Angeles Ana M. Hernández-Vega Tamara Rosenbaum Recent advances on the structure and the function relationships of the TRPV4 ion channel Channels Ion channel TRPV4 structure Cryo-EM 4α-PDD HC-067047 |
| title | Recent advances on the structure and the function relationships of the TRPV4 ion channel |
| title_full | Recent advances on the structure and the function relationships of the TRPV4 ion channel |
| title_fullStr | Recent advances on the structure and the function relationships of the TRPV4 ion channel |
| title_full_unstemmed | Recent advances on the structure and the function relationships of the TRPV4 ion channel |
| title_short | Recent advances on the structure and the function relationships of the TRPV4 ion channel |
| title_sort | recent advances on the structure and the function relationships of the trpv4 ion channel |
| topic | Ion channel TRPV4 structure Cryo-EM 4α-PDD HC-067047 |
| url | https://www.tandfonline.com/doi/10.1080/19336950.2024.2313323 |
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