期刊
ELIFE
卷 7, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.41845
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资金
- Howard Hughes Medical Institute
- National Institute of Neurological Disorders and Stroke [1R35NS105067]
- Ray Thomas Edwards Foundation
- Wellcome [208361/Z/17/Z]
- Biotechnology and Biological Sciences Research Council [BB/N000145/1, BB/R00126X/1]
- Engineering and Physical Sciences Research Council [EP/R004722/1]
- Jane Coffin Childs Memorial Fund for Medical Research
- Skaggs-Oxford Scholarship
- Croucher Foundation
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R35NS105067] Funding Source: NIH RePORTER
- BBSRC [BB/R00126X/1, BB/N000145/1] Funding Source: UKRI
- EPSRC [EP/R004722/1, EP/L000253/1] Funding Source: UKRI
Mechanically activated ion channels underlie touch, hearing, shear-stress sensing, and response to turgor pressure. OSCA/TMEM63s are a newly-identified family of eukaryotic mechanically activated ion channels opened by membrane tension. The structural underpinnings of OSCA/TMEM63 function are not explored. Here, we elucidate high resolution cryo-electron microscopy structures of OSCA1.2, revealing a dimeric architecture containing eleven transmembrane helices per subunit and surprising topological similarities to TMEM16 proteins. We locate the ion permeation pathway within each subunit by demonstrating that a conserved acidic residue is a determinant of channel conductance. Molecular dynamics simulations reveal membrane interactions, suggesting the role of lipids in OSCA1.2 gating. These results lay a foundation to decipher how the structural organization of OSCA/TMEM63 is suited for their roles as MA ion channels.
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