Journal article
Lizard and frog prestin: evolutionary insight into functional changes
PloS one, Vol.8(1), pp.e54388-e54388
2013
DOI: 10.1371/journal.pone.0054388
PMCID: PMC3546999
PMID: 23342145
Abstract
The plasma membrane of mammalian cochlear outer hair cells contains prestin, a unique motor protein. Prestin is the fifth member of the solute carrier protein 26A family. Orthologs of prestin are also found in the ear of non-mammalian vertebrates such as zebrafish and chicken. However, these orthologs are electrogenic anion exchangers/transporters with no motor function. Amphibian and reptilian lineages represent phylogenic branches in the evolution of tetrapods and subsequent amniotes. Comparison of the peptide sequences and functional properties of these prestin orthologs offer new insights into prestin evolution. With the recent availability of the lizard and frog genome sequences, we examined amino acid sequence and function of lizard and frog prestins to determine how they are functionally and structurally different from prestins of mammals and other non-mammals. Somatic motility, voltage-dependent nonlinear capacitance (NLC), the two hallmarks of prestin function, and transport capability were measured in transfected human embryonic kidney cells using voltage-clamp and radioisotope techniques. We demonstrated that while the transport capability of lizard and frog prestin was compatible to that of chicken prestin, the NLC of lizard prestin was more robust than that of chicken's and was close to that of platypus. However, unlike platypus prestin which has acquired motor capability, lizard or frog prestin did not demonstrate motor capability. Lizard and frog prestins do not possess the same 11-amino-acid motif that is likely the structural adaptation for motor function in mammals. Thus, lizard and frog prestins appear to be functionally more advanced than that of chicken prestin, although motor capability is not yet acquired.
Details
- Title: Subtitle
- Lizard and frog prestin: evolutionary insight into functional changes
- Creators
- Jie Tang - Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, Nebraska, United States of AmericaJason L PeckaBernd FritzschKirk W BeiselDavid Z Z He
- Resource Type
- Journal article
- Publication Details
- PloS one, Vol.8(1), pp.e54388-e54388
- DOI
- 10.1371/journal.pone.0054388
- PMID
- 23342145
- PMCID
- PMC3546999
- NLM abbreviation
- PLoS One
- ISSN
- 1932-6203
- eISSN
- 1932-6203
- Publisher
- Public Library of Science; United States
- Grant note
- R01 DC004696 / NIDCD NIH HHS P20 RR018788 / NCRR NIH HHS R01 DC008649 / NIDCD NIH HHS 2P20 RR18788 / NCRR NIH HHS C06 RR017417 / NCRR NIH HHS RR17417-01 / NCRR NIH HHS
- Language
- English
- Date published
- 2013
- Academic Unit
- Iowa Neuroscience Institute; Biology; Craniofacial Anomalies Research Center
- Record Identifier
- 9984070647102771
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