8tdl
Cryo-EM structure of the wild-type AtMSL10 in saposin
Structural highlights
FunctionMSL10_ARATH Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer.[1] [2] Publication Abstract from PubMedPlants are challenged by drastically different osmotic environments during growth and development. Adaptation to these environments often involves mechanosensitive ion channels that can detect and respond to mechanical force. In the model plant Arabidopsis thaliana, the mechanosensitive channel MSL10 plays a crucial role in hypo-osmotic shock adaptation and programmed cell death induction, but the molecular basis of channel function remains poorly understood. Here, we report a structural and electrophysiological analysis of MSL10. The cryo-electron microscopy structures reveal a distinct heptameric channel assembly. Structures of the wild-type channel in detergent and lipid environments, and in the absence of membrane tension, capture an open conformation. Furthermore, structural analysis of a non-conductive mutant channel demonstrates that reorientation of phenylalanine side chains alone, without main chain rearrangements, may generate the hydrophobic gate. Together, these results reveal a distinct gating mechanism and advance our understanding of mechanotransduction. Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10.,Zhang J, Maksaev G, Yuan P Nat Commun. 2023 Oct 7;14(1):6284. doi: 10.1038/s41467-023-42117-5. PMID:37805510[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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