Reciprocal electromechanical properties of rat prestin: the motor molecule from rat outer hair cells.
Cochlear outer hair cells (OHCs) are responsible for the exquisite sensitivity, dynamic range, and frequency-resolving capacity of the mammalian hearing organ. These unique cells respond to an electrical stimulus with a cycle-by-cycle change in cell length that is mediated by molecular motors in the cells' basolateral membrane. Recent work identified prestin, a protein with similarity to pendrin-related anion transporters, as the OHC motor molecule. Here we show that heterologously expressed prestin from rat OHCs (rprestin) exhibits reciprocal electromechanical properties as known for the OHC motor protein. Upon electrical stimulation in the microchamber configuration, rprestin generates mechanical force with constant amplitude and phase up to a stimulus frequency of at least 20 kHz. Mechanical stimulation of rprestin in excised outside-out patches shifts the voltage dependence of the nonlinear capacitance characterizing the electrical properties of the molecule. The results indicate that rprestin is a molecular motor that displays reciprocal electromechanical properties over the entire frequency range relevant for mammalian hearing.
Department of Physiology II, Ob dem Himmelreich 7, 72074 Tübingen, Germany.
J
J
Ludwig
D
D
Oliver
G
G
Frank
N
N
Klöcker
A W
AW
Gummer
B
B
Fakler
D000595:Amino Acid Sequence; D000818:Animals; D027321:Anion Transport Proteins; D003001:Cloning, Molecular; D003051:Cochlea / Q000166:cytology; D004594:Electrophysiology; D018072:Hair Cells, Auditory, Outer / Q000737:chemistry* / Q000502:physiology; D007150:Immunohistochemistry; D008969:Molecular Sequence Data; D009893:Opossums; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D051381:Rats; D017386:Sequence Homology, Amino Acid; D000076988:Sulfate Transporters
D027321:Anion Transport Proteins; D011506:Proteins; C409207:Slc26a5 protein, rat; D000076988:Sulfate Transporters