Cochlear transduction: from models to molecules and back again.
The strides made over the last few years towards understanding many details of cochlear function still leave a number of issues unresolved. Integrating the information from molecular, genetic and, increasingly, genomic sources requires models that provide close matching between data and theory. For both theoretical and experimental reasons, the difficult area in cochlear physiology has been to understand how sensory transduction operates at the basal end of the mammalian cochlea. The identification of candidate motor proteins in outer hair cells (OHCs) draws attention to the question of whether we understand cochlear tuning. Nevertheless, the association of the cloned motor protein 'prestin' with an anion transporter superfamily provides clues about the molecular nature of the OHC motor in the basolateral membrane, the utilisation of chloride in hair cells and the long-term stability of small basal turn cochlear hair cells.
Ashmore
Jonathan F
JF
Department of Physiology, University College London, UK. j.ashmore@ucl.ac.uk
Chambard
Jean-Marie
JM
Richmond
Sarah
S
D000818:Animals; D027321:Anion Transport Proteins; D003051:Cochlea / Q000502:physiology*; D015870:Gene Expression / Q000502:physiology; D051296:Glucose Transporter Type 5; D018072:Hair Cells, Auditory, Outer / Q000502:physiology; D006309:Hearing / Q000502:physiology*; D006801:Humans; D020409:Molecular Motor Proteins / Q000502:physiology; D009004:Monosaccharide Transport Proteins / Q000235:genetics; D011506:Proteins / Q000235:genetics; D015398:Signal Transduction / Q000502:physiology*; D000076988:Sulfate Transporters
D027321:Anion Transport Proteins; D051296:Glucose Transporter Type 5; D020409:Molecular Motor Proteins; D009004:Monosaccharide Transport Proteins; D011506:Proteins; C498719:SLC26A5 protein, human; D000076988:Sulfate Transporters