Prestin modulates mechanics and electromechanical force of the plasma membrane.
The voltage-dependent movement, or electromotility, of cochlear outer hair cells contributes to cochlear amplification in mammalian hearing. Outer hair-cell electromotility involves a membrane-based motor in which the membrane protein prestin plays a central role. We have investigated the contribution of prestin to the mechanics and electromechanical force (EMF) generation of the membrane using membrane tethers formed from human embryonic kidney (HEK) cells. Several measures of membrane tether mechanics are greater in tethers pulled from HEK cells transfected with prestin when compared to control untransfected HEK cells. A single point mutation of alanine to tryptophan (A100W) in prestin eliminates prestin-associated charge movement and diminishes EMF but does not alter passive membrane mechanics. These results suggest that prestin-associated charge transfer is necessary for maximal EMF generation by the membrane.
Zhang
Rui
R
Applied Physics Graduate Program, Rice University, Houston, Texas, USA.
Qian
Feng
F
Rajagopalan
Lavanya
L
Pereira
Fred A
FA
Brownell
William E
WE
Anvari
Bahman
B
D027321:Anion Transport Proteins / Q000502:physiology*; D002460:Cell Line; D002462:Cell Membrane / Q000502:physiology*; D006801:Humans; D007668:Kidney / Q000502:physiology*; D040542:Mechanotransduction, Cellular / Q000502:physiology*; D008560:Membrane Fluidity / Q000502:physiology; D008564:Membrane Potentials / Q000502:physiology*; D020409:Molecular Motor Proteins / Q000502:physiology*; D013314:Stress, Mechanical; D000076988:Sulfate Transporters
D027321:Anion Transport Proteins; D020409:Molecular Motor Proteins; C498719:SLC26A5 protein, human; D000076988:Sulfate Transporters