Abstract
In a recent paper published in the Biochemical Journal, Lolli et al. presented evidence that the C-terminal STAS (sulfate transporter and anti-sigma factor antagonist) domain of the motor protein prestin possesses an anion-binding site. This discovery might shed light on an aspect of the function of this mysterious and fascinating protein that is crucial for the human hearing system.
Highlights
Prestin [SLC26A5] belongs to the ubiquitous solute carrier 26 (SLC26)/sulfate permease (SulP) family of anion exchangers and is one of ten SLC26A transporters that have been identified in animals, most of which are known to transport anions across membranes either in an electroneutral or electrogenic manner [1]
Genes encoding four members of the SCL26A protein family have been identified as disease genes: mutations in the genes encoding SLC26A2/DTD, SLC26A3/DRA, SLC26A4/pendrin and SLC26A5/prestin are associated with diastrophic dysplasia, congenital chloride-losing diarrhoea, Pendred syndrome and human deafness, respectively [1]
Prestin is a member of a mammalian anionexchanger family, it apparently has a very different function in cochlear outer hair cell (OHC), where it is densely packed in the basolateral membrane
Summary
Prestin [SLC26A5 (solute carrier 26A5)] belongs to the ubiquitous SLC26/SulP (sulfate permease) family of anion exchangers and is one of ten SLC26A transporters that have been identified in animals, most of which are known to transport anions across membranes either in an electroneutral or electrogenic manner [1]. OHCs in mammals have the ability to alter their cell length in response to changes in membrane potential triggered by incoming sound waves.
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