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The Conserved Tetrameric Subunit Stoichiometry of Slc26 Proteins

Published online by Cambridge University Press:  03 May 2013

Richard Hallworth ,
Kelsey Stark ,
Lyandysha Zholudeva ,
Benjamin B. Currall  and
Michael G. Nichols
Richard Hallworth*
Affiliation:
Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, NE 68178, USA
Kelsey Stark
Affiliation:
Department of Biology, Doane College, Crete, NE 68333, USA
Lyandysha Zholudeva
Affiliation:
Department of Physics, Creighton University, Omaha, NE 68178, USA
Benjamin B. Currall
Affiliation:
Department of Obstetrics, Gynecology, and Reproductive Biology, Brigham and Women's Hospital, Boston, MA 02115, USA
Michael G. Nichols
Affiliation:
Department of Physics, Creighton University, Omaha, NE 68178, USA
*
*Corresponding author. E-mail: hallw@creighton.edu
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Abstract

The Slc26 family proteins, with one possible exception, transport anions across membranes in a wide variety of tissues in vertebrates, invertebrates, and plants. Mutations in human members of the family are a significant cause of disease. Slc26 family proteins are thought to be oligomers, but their stoichiometry of association is in dispute. A recent study, using sequential bleaching of single fluorophore-coupled molecules in membrane fragments, demonstrated that mammalian Slc26a5 (prestin) is a tetramer. In this article, the stoichiometry of two nonmammalian prestins and three human SLC26 proteins has been analyzed by the same method, including the evolutionarily-distant SLC26A11. The analysis showed that tetramerization is common and likely to be ubiquitous among Slc26 proteins, at least in vertebrates. The implication of the findings is that tetramerization is present for functional reasons.

Keywords

hair cellouter hair cellprestinpendrinSlc26
Type
Omaha Imaging Symposium
Information
Microscopy and Microanalysis , Volume 19 , Issue 4 , August 2013 , pp. 799 - 807
Copyright
Copyright © Microscopy Society of America 2013 

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