NDLI: Expression of prestin-homologous solute carrier (SLC26) in auditory organs of nonmammalian vertebrates and insects.

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Expression of prestin-homologous solute carrier (SLC26) in auditory organs of nonmammalian vertebrates and insects.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Meier, Alexandra Kohler, Hanni Winter, Harald Weber, Thomas Hendrich, Oliver Rohbock, Karin Robert, Daniel Gopfert, Martin C. Zimmermann, Ulrike Knipper, Marlies
Description	Author Affiliation: Weber T ( Department of Otolaryngology, Tübingen Hearing Research Center, Molecular Neurobiology, Elfriede-Aulhorn-Strasse 5, D-72076 Tübingen, Germany.);
Abstract	Prestin, the fifth member of the anion transporter family SLC26, is the outer hair cell molecular motor thought to be responsible for active mechanical amplification in the mammalian cochlea. Active amplification is present in a variety of other auditory systems, yet the prevailing view is that prestin is a motor molecule unique to mammalian ears. Here we identify prestin-related SLC26 proteins that are expressed in the auditory organs of nonmammalian vertebrates and insects. Sequence comparisons revealed the presence of SLC26 proteins in fish (Danio, GenBank accession no. AY278118, and Anguilla, GenBank accession no. BAC16761), mosquitoes (Anopheles, GenBank accession nos. EAA07232 and EAA07052), and flies (Drosophila, GenBank accession no. AAF49285). The fly and zebrafish homologues were cloned and, by using in situ hybridization, shown to be expressed in the auditory organs. In mosquitoes, in turn, the expression of prestin homologues was demonstrated for the auditory organ by using highly specific riboprobes against rat prestin. We conclude that prestin-related SLC26 proteins are widespread, possibly ancestral, constituents of auditory organs and are likely to serve salient roles in mammals and across taxa.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	13
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Anion Transport Proteins Biosynthesis Carrier Proteins Membrane Transport Proteins Protein Biosynthesis Algorithms Amino Acid Sequence Anguilla Animals Chemistry Anopheles Cloning, Molecular Cochlea Metabolism Drosophila Melanogaster Epithelium In Situ Hybridization Mice Mice, Inbred C57BL Molecular Motor Proteins Molecular Sequence Data Phylogeny Proteins RNA, Messenger Rats, Wistar Sequence Analysis, DNA Sequence Homology, Amino Acid Zebrafish Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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