title: Transduction of membrane tension by the ion channel alamethicin.
abstract: Mechanoelectrical transduction in biological cells is generally attributed to tension-sensitive ion channels, but their mechanisms and physiology remain controversial due to the elusiveness of the channel proteins and potential cytoskeletal interactions. Our discovery of membrane tension sensitivity in ion channels formed by the protein alamethicin reconstituted into pure lipid membranes has demonstrated two simple physical mechanisms of cytoskeleton-independent transduction. Single channel analysis has shown that membrane tension energizes mechanical work for changes of conductance state equal to tension times the associated increase in membrane area. Results show a approximately 40 A2 increase in pore area and transfer of an 80-A2 polypeptide into the membrane. Both mechanisms may be implicated in mechanical signal transduction by cells.
authors.affiliation: Department of Physics, Cornell University, Ithaca, New York 14853.
authors.forename: L R
authors.initials: LR
authors.lastname: Opsahl
authors.forename: W W
authors.initials: WW
authors.lastname: Webb
mesh_terms: D000408:Alamethicin / Q000737:chemistry*; D004548:Elasticity; D004594:Electrophysiology; D007473:Ion Channels / Q000502:physiology*; D007700:Kinetics; D008433:Mathematics; D008954:Models, Biological; D013314:Stress, Mechanical; D013997:Time Factors
chemical_list: D007473:Ion Channels; D000408:Alamethicin