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TitleThe lipid-mediated mechanism of mechanosensitive channel MscS inactivation.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateSep 10, 2025
AuthorsElissa Moller / Madolyn Britt / Fei Zhou / Hyojik Yang / Andriy Anishkin / Robert Ernst / Juan M Vanegas / Sergei Sukharev / Doreen Matthies
PubMed AbstractInterpretations of experimental conformations of mechanosensitive channels gated by 'force from lipids' become more reliable when native lipids are preserved in the structures. MscS is an adaptive ...Interpretations of experimental conformations of mechanosensitive channels gated by 'force from lipids' become more reliable when native lipids are preserved in the structures. MscS is an adaptive osmolyte release valve that regulates turgor in osmotically stressed cells. MscS promptly opens under abrupt super-threshold tensions in the membrane, but at lower and more gradually applied tensions, it silently inactivates from the closed state. A central question has been whether to assign the commonly observed non-conductive conformation with splayed peripheral helices to a closed or inactivated state. We present a 3-Å MscS cryo-EM structure obtained in Glyco-DIBMA polymers, which avoid complete lipid removal. Within the complex, we observe densities for endogenous phospholipids intercalating between the peripheral and pore-lining helices. The lipidomic analysis shows a 2-3 fold enrichment of phosphatidylglycerol in Glyco-DIBMA-extracted MscS samples. The computed pressure of these lipids on the protein surface enforces the characteristic kinks in the pore-lining helices, sterically stabilizing the separation of the peripheral helices. Mutations of residues coordinating lipids in the crevices eliminate inactivation, allowing us to classify this group of structures as the inactivated state. Our study reveals a novel inactivation mechanism in which intercalated lipids physically decouple the tension-sensing helices from the gate.
External linksbioRxiv / PubMed:38328078 / PubMed Central
MethodsEM (single particle)
Resolution2.99 Å
Structure data

71088

9p0n

EMDB-71088, PDB-9p0n:
MscS in Glyco-DIBMA Native Nanodiscs (C7 symmetry)
Method: EM (single particle) / Resolution: 2.99 Å

Chemicals

ChemComp-D21:
(2R)-1-(hexadecanoyloxy)-3-(phosphonooxy)propan-2-yl (9Z)-octadec-9-enoate

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsMEMBRANE PROTEIN / mechanosensitive channel / native nanodisc / polymer / Glyco-DIBMA / cryo-EM / lipid

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