Prestin (SLC26A5) is encoded by the SLC26A5 gene and is also known as Solute carrier family 26 member 5. It belongs to the SLC26 family of membrane proteins, which combine a variety of functions within a conserved molecular scaffold Prestin (SLC26A5) is the transmembrane protein that confers voltage-dependent mechanical activity, often referred to as somatic electromotility, on auditory outer hair cells. SLC26A5 represents a new type of molecular motor, which is likely to be of great interest to molecular cell biologists.
|Basic Information of SLC26A5|
|Aliases||Solute carrier family 26 member 5|
|Organism||Homo sapiens (Human)|
SLC26A5 is a new type of biological motor. It is entirely different from the well-known and much-studied classical cellular motors in that its function is not based on enzymatic processes, but on direct voltage-to-displacement conversion. SLC26A5 is a new type of biological motor and the action of SLC26A5 is also orders of magnitude faster than that of any other cellular motor protein, as it functions at microsecond rates. The functional properties of SLC26A5 strongly support the concept of a single protein acting as an electromechanical transducer in outer hair cells. SLC26A5 is a direct voltage-to-force converter, which uses cytoplasmic anions as extrinsic voltage sensors and can operate at microsecond rates. As SLC26A5 mediates changes in outer hair cell length in response to membrane potential variations, it might be responsible for sound amplification in the mammalian hearing organ. SLC26A5 could also behave as a sensor of mechanical stress, or operate as a voltage-controlled capacitor in electrical nanocircuits. Finally, the remarkable properties of SLC26A5 make it a candidate for future nanotechnology applications.
Fig .1 A structural model for the transmembrane region of prestin (SLC26A5). (Takahashi, 2016)
This article provides experimental evidence that supports a causal relationship between the R130S mutation in the prestin (SLC26A5) gene and hearing loss found in patients with this missense mutation.
This article summarizes the functions and characterizations of prestin (SLC26A5), and prestin mediates changes in outer hair cell length in response to membrane potential variations, it might be responsible for sound amplification in the mammalian hearing organ.
This article reviews recent advances of the structural and functional properties of prestin (SLC26A5) with focus on the areas that are critical but still controversial in understanding the molecular mechanism of how prestin (SLC26A5) works: The structural domains for voltage sensing and interaction with anions and for conformational change. Future research directions and potential application of prestin (SLC26A5) are also discussed.
This article demonstrates that prestin (SLC26A5) does not affect the chloride conductance of CFTR, which is activated by cAMP and is capable of enhancing voltage-dependent charge displacement, a signature of cochlear outer hair cells motility.
The data of this article indicate that functional prestin (SLC26A5) is up-regulated in residual outer hair cells after noise exposure. Meanwhile, prestin (SLC26A5) increases in an attempt to partially compensate for reduced force production because of missing outer hair cells.
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