title: The conserved tetrameric subunit stoichiometry of Slc26 proteins.
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.
authors: Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, NE 68178, USA. hallw@creighton.edu
authors: Richard
authors: R
authors: Hallworth
authors: Kelsey
authors: K
authors: Stark
authors: Lyandysha
authors: L
authors: Zholudeva
authors: Benjamin B
authors: BB
authors: Currall
authors: Michael G
authors: MG
authors: Nichols
mesh_terms: D000818:Animals; D027321:Anion Transport Proteins / Q000737:chemistry* / Q000378:metabolism*; D002460:Cell Line; D005849:Gerbillinae; D006801:Humans; D008856:Microscopy, Fluorescence; D055503:Protein Multimerization; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism
chemical_list: D027321:Anion Transport Proteins; D021122:Protein Subunits
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