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.
| Original language | English |
|---|---|
| Pages (from-to) | 799-807 |
| Number of pages | 9 |
| Journal | Microscopy and Microanalysis |
| Volume | 19 |
| Issue number | 4 |
| DOIs | |
| State | Published - Aug 2013 |
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All Science Journal Classification (ASJC) codes
- Instrumentation
Cite this
The conserved tetrameric subunit stoichiometry of Slc26 proteins. / Hallworth, Richard J.; Stark, Kelsey; Zholudeva, Lyandysha; Currall, Benjamin B.; Nichols, Michael G.
In: Microscopy and Microanalysis, Vol. 19, No. 4, 08.2013, p. 799-807.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The conserved tetrameric subunit stoichiometry of Slc26 proteins
AU - Hallworth, Richard J.
AU - Stark, Kelsey
AU - Zholudeva, Lyandysha
AU - Currall, Benjamin B.
AU - Nichols, Michael G.
PY - 2013/8
Y1 - 2013/8
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=84880251609&partnerID=8YFLogxK
U2 - 10.1017/S1431927613000457
DO - 10.1017/S1431927613000457
M3 - Article
C2 - 23642772
AN - SCOPUS:84880251609
VL - 19
SP - 799
EP - 807
JO - Microscopy and Microanalysis
JF - Microscopy and Microanalysis
SN - 1431-9276
IS - 4
ER -