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PreprintCited by 20Ion channel regulation and functionIon Channels and ReceptorsProtein Structure and Dynamics

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

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Jojoa-Cruz, Sebastian, Burendei, Batuujin, Lee, Wen-Hsin, Ward, Andrew B.·2023·Structure
DOI 10.1101/2023.06.15.545135PMC PMC10872982

Preprint — published as 10.1016/j.str.2023.11.009 · Paper page

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Abstract

Summary: 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.

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Metadata

Authors
Jojoa-Cruz, S., Burendei, B., Lee, W.-H., & Ward, A. B.
Affiliations
Scripps Research Institute (US)
Corresponding author
Ward, Andrew B.
ORCID
Venue
Structure
Publisher
openRxiv
Published
2023-06-15
Volume
32
Issue
2
Pages
157-167.e5
ISSN
0969-2126 (ISSN-L)
DOI
10.1101/2023.06.15.545135
PMC
PMC10872982
OpenAlex
W4389818930
Cited by
20
References
1
Citations by year
2026: 2 · 2025: 7 · 2024: 6 · 2023: 5
FWCI
1.78
Type
journal article
Language
en
Open access
Locations
  • Structure (publishedVersion)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • PubMed Central (submittedVersion, cc-by)
Funders
  • Ray Thomas Edwards Foundation
  • National Institutes of Health
  • University of California, San Francisco (P41-GM103311, R01-GM129325)
  • National Heart, Lung, and Blood Institute (R01HL143297)
  • National Institute of General Medical Sciences (P41GM103311, R01GM129325)
  • National Institute of Allergy and Infectious Diseases
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
  • Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
mechanosensitive ion channels, Arabidopsis thaliana, transmembrane domain, conformational heterogeneity, mechanosensing, pore constriction, peptidisc

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