{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cox CD"],"funding":["NHLBI NIH HHS"],"pagination":["10366"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4735864"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7"],"pubmed_abstract":["Mechanosensitive ion channels are force-transducing enzymes that couple mechanical stimuli to ion flux. Understanding the gating mechanism of mechanosensitive channels is challenging because the stimulus seen by the channel reflects forces shared between the membrane, cytoskeleton and extracellular matrix. Here we examine whether the mechanosensitive channel PIEZO1 is activated by force-transmission through the bilayer. To achieve this, we generate HEK293 cell membrane blebs largely free of cytoskeleton. Using the bacterial channel MscL, we calibrate the bilayer tension demonstrating that activation of MscL in blebs is identical to that in reconstituted bilayers. Utilizing a novel PIEZO1-GFP fusion, we then show PIEZO1 is activated by bilayer tension in bleb membranes, gating at lower pres"],"journal":["Nature communications"],"pubmed_title":["Removal of the mechanoprotective influence of the cytoskeleton reveals PIEZO1 is gated by bilayer tension."],"pmcid":["PMC4735864"],"funding_grant_id":["R01 HL054887","NIH 5R01HL054887"],"pubmed_authors":["Ziegler L","Cox CD","Nikolova-Krstevski V","Hartley S","Gottlieb PA","Bae C","Sachs F","Martinac B","Rohde PR","Ng CA"],"additional_accession":[]},"is_claimable":false,"name":"Removal of the mechanoprotective influence of the cytoskeleton reveals PIEZO1 is gated by bilayer tension.","description":"Mechanosensitive ion channels are force-transducing enzymes that couple mechanical stimuli to ion flux. Understanding the gating mechanism of mechanosensitive channels is challenging because the stimulus seen by the channel reflects forces shared between the membrane, cytoskeleton and extracellular matrix. Here we examine whether the mechanosensitive channel PIEZO1 is activated by force-transmission through the bilayer. To achieve this, we generate HEK293 cell membrane blebs largely free of cytoskeleton. Using the bacterial channel MscL, we calibrate the bilayer tension demonstrating that activation of MscL in blebs is identical to that in reconstituted bilayers. Utilizing a novel PIEZO1-GFP fusion, we then show PIEZO1 is activated by bilayer tension in bleb membranes, gating at lower pres","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jan","modification":"2025-04-22T19:56:10.152Z","creation":"2019-03-27T02:08:02Z"},"accession":"S-EPMC4735864","cross_references":{"pubmed":["26785635"],"doi":["10.1038/ncomms10366"]}}