Cargando…

Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain

Members of the OSCA/TMEM63 are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are potentially involved in mechanosensation. However, these structures are all in a similar state and information abou...

Descripción completa

Detalles Bibliográficos
Autores principales: Jojoa-Cruz, Sebastian, Burendei, Batuujin, Lee, Wen-Hsin, Ward, Andrew B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10312710/
https://www.ncbi.nlm.nih.gov/pubmed/37398040
http://dx.doi.org/10.1101/2023.06.15.545135
_version_ 1785066973902667776
author Jojoa-Cruz, Sebastian
Burendei, Batuujin
Lee, Wen-Hsin
Ward, Andrew B.
author_facet Jojoa-Cruz, Sebastian
Burendei, Batuujin
Lee, Wen-Hsin
Ward, Andrew B.
author_sort Jojoa-Cruz, Sebastian
collection PubMed
description Members of the OSCA/TMEM63 are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are potentially involved in mechanosensation. However, these structures are all in a similar state and information about the motion of different elements of the structure is limited, preventing a deeper understanding of how these channels work. Here, we used cryo-electron microscopy to determine high resolution structures of Arabidopsis thaliana OSCA1.2 and OSCA2.3 in peptidiscs. The structure of OSCA1.2 resembles previous structures of the same protein in different environments. Yet, in OSCA2.3 the TM6a-TM7 linker constricts the pore on its cytoplasmic side, revealing conformational heterogeneity within the OSCA family. Furthermore, coevolutionary sequence analysis uncovered a conserved interaction between TM6a-TM7 linker and the Beam-Like Domain. Our results support the involvement of TM6a-TM7 in mechanosensation and potentially in the diverse response of OSCA channels to mechanical stimuli.
format Online
Article
Text
id pubmed-10312710
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher Cold Spring Harbor Laboratory
record_format MEDLINE/PubMed
spelling pubmed-103127102023-07-01 Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain Jojoa-Cruz, Sebastian Burendei, Batuujin Lee, Wen-Hsin Ward, Andrew B. bioRxiv Article Members of the OSCA/TMEM63 are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are potentially involved in mechanosensation. However, these structures are all in a similar state and information about the motion of different elements of the structure is limited, preventing a deeper understanding of how these channels work. Here, we used cryo-electron microscopy to determine high resolution structures of Arabidopsis thaliana OSCA1.2 and OSCA2.3 in peptidiscs. The structure of OSCA1.2 resembles previous structures of the same protein in different environments. Yet, in OSCA2.3 the TM6a-TM7 linker constricts the pore on its cytoplasmic side, revealing conformational heterogeneity within the OSCA family. Furthermore, coevolutionary sequence analysis uncovered a conserved interaction between TM6a-TM7 linker and the Beam-Like Domain. Our results support the involvement of TM6a-TM7 in mechanosensation and potentially in the diverse response of OSCA channels to mechanical stimuli. Cold Spring Harbor Laboratory 2023-06-15 /pmc/articles/PMC10312710/ /pubmed/37398040 http://dx.doi.org/10.1101/2023.06.15.545135 Text en https://creativecommons.org/licenses/by/4.0/This work is licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/) , which allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use.
spellingShingle Article
Jojoa-Cruz, Sebastian
Burendei, Batuujin
Lee, Wen-Hsin
Ward, Andrew B.
Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain
title Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain
title_full Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain
title_fullStr Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain
title_full_unstemmed Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain
title_short Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain
title_sort structure of mechanically activated ion channel osca2.3 reveals mobile elements in the transmembrane domain
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10312710/
https://www.ncbi.nlm.nih.gov/pubmed/37398040
http://dx.doi.org/10.1101/2023.06.15.545135
work_keys_str_mv AT jojoacruzsebastian structureofmechanicallyactivatedionchannelosca23revealsmobileelementsinthetransmembranedomain
AT burendeibatuujin structureofmechanicallyactivatedionchannelosca23revealsmobileelementsinthetransmembranedomain
AT leewenhsin structureofmechanicallyactivatedionchannelosca23revealsmobileelementsinthetransmembranedomain
AT wardandrewb structureofmechanicallyactivatedionchannelosca23revealsmobileelementsinthetransmembranedomain