Nature communications, 2020-07, Vol.11 (1), p.3690-3690, Article 3690
2020
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Titel
- Structural mechanism for gating of a eukaryotic mechanosensitive channel of small conductance
- Ist Teil von
- Nature communications, 2020-07, Vol.11 (1), p.3690-3690, Article 3690
- Ort / Verlag
- England: Nature Publishing Group
- Erscheinungsjahr
- 2020
- Quelle
- Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
- Beschreibungen/Notizen
- Mechanosensitive ion channels transduce physical force into electrochemical signaling that underlies an array of fundamental physiological processes, including hearing, touch, proprioception, osmoregulation, and morphogenesis. The mechanosensitive channels of small conductance (MscS) constitute a remarkably diverse superfamily of channels critical for management of osmotic pressure. Here, we present cryo-electron microscopy structures of a MscS homolog from Arabidopsis thaliana, MSL1, presumably in both the closed and open states. The heptameric MSL1 channel contains an unusual bowl-shaped transmembrane region, which is reminiscent of the evolutionarily and architecturally unrelated mechanosensitive Piezo channels. Upon channel opening, the curved transmembrane domain of MSL1 flattens and expands. Our structures, in combination with functional analyses, delineate a structural mechanism by which mechanosensitive channels open under increased membrane tension. Further, the shared structural feature between unrelated channels suggests the possibility of a unified mechanical gating mechanism stemming from membrane deformation induced by a non-planar transmembrane domain.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 2041-1723eISSN: 2041-1723DOI: 10.1038/s41467-020-17538-1Titel-ID: cdi_doaj_primary_oai_doaj_org_article_24278fd6df614c24883c81fc709a6580
- Format
- –
- Schlagworte
- Arabidopsis - metabolism, Arabidopsis Proteins - chemistry, Arabidopsis Proteins - metabolism, Arabidopsis Proteins - ultrastructure, Channel gating, Channel opening, Conductance, Deformation mechanisms, Domains, Electrochemistry, Electron microscopy, Escherichia coli Proteins - chemistry, Escherichia coli Proteins - metabolism, Eukaryota - metabolism, Hearing, Homology, Ion Channel Gating, Ion channels, Ion Channels - chemistry, Ion Channels - metabolism, Ion Channels - ultrastructure, Mechanosensitive channels, Mechanotransduction, Cellular, Membranes, Microscopy, Models, Molecular, Morphogenesis, Mutant Proteins - chemistry, Mutant Proteins - metabolism, Osmoregulation, Osmosis, Osmotic pressure, Proprioception, Protein Domains, Protein Structure, Secondary, Resistance, Signaling, Touch, Transmission electron microscopy