title: Membrane thickness sensitivity of prestin orthologs: the evolution of a piezoelectric protein.
abstract: How proteins evolve new functionality is an important question in biology; prestin (SLC26A5) is a case in point. Prestin drives outer hair cell somatic motility and amplifies mechanical vibrations in the mammalian cochlea. The motility of mammalian prestin is analogous to piezoelectricity, in which charge transfer is coupled to changes in membrane area occupied by the protein. Intriguingly, nonmammalian prestin orthologs function as anion exchangers but are apparently nonmotile. We previously found that mammalian prestin is sensitive to membrane thickness, suggesting that prestin's extended conformation has a thinner hydrophobic height in the lipid bilayer. Because prestin-based motility is a mammalian specialization, we initially hypothesized that nonmotile prestin orthologs, while functioning as anion transporters, should be much less sensitive to membrane thickness. We found the exact opposite to be true. Chicken prestin was the most sensitive to thickness changes, displaying the largest shift in voltage dependence. Platypus prestin displayed an intermediate response to membrane thickness and gerbil prestin was the least sensitive. To explain these observations, we present a theory where force production, rather than displacement, was selected for the evolution of prestin as a piezoelectric membrane motor.
authors.affiliation: Biophysics Section, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Rockville, Maryland, USA.
authors.forename: Chisako
authors.initials: C
authors.lastname: Izumi
authors.forename: Jonathan E
authors.initials: JE
authors.lastname: Bird
authors.forename: Kuni H
authors.initials: KH
authors.lastname: Iwasa
mesh_terms: D000818:Animals; D001696:Biomechanical Phenomena; D016466:CHO Cells; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism; D002645:Chickens; D006224:Cricetinae; D003412:Cricetulus; D025802:Electric Capacitance; D019143:Evolution, Molecular; D005849:Gerbillinae; D057809:HEK293 Cells; D006801:Humans; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D010987:Platypus; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
chemical_list: D026901:Membrane Transport Proteins