SLC26 Anion Transporters

Geertsma, Eric R.; Oliver, Dominik

doi:10.1007/164_2023_698

Cited by 3 publications

(1 citation statement)

References 279 publications

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“…The SLC26 family contains ten human members that - with the exception of SLC26A5/prestin, the motor protein in outer hair cells (1) - function as transporters/channels for a broad range of anionic substrates (2,3). SLC26A1, SLC26A2, and SLC26A8 electroneutrally exchange SO 4 2- or oxalate 2- with Cl - or OH - .…”

Section: Introductionmentioning

confidence: 99%

Oligomerization and cellular localization of SLC26A11

Bungert-Plümke,

Guzman,

Fahlke

2024

Preprint

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The solute carrier family 26 (SLC26) encompasses multifunctional anion exchangers in all kingdoms of life. SLC26 proteins are known to assemble as dimers, and co-expression of multiple isoforms in certain cells raises the question of whether different SLC26s can assemble into hetero-dimers. We focused on SLC26A11, a broadly expressed isoform that differs from other isoforms in its subcellular localization. Whereas the vast majority of SLC26-FP fusion proteins, i.e., SLC26A1, SLC26A2, SlC26A3, SLC26A4/pendrin, SLC26A5/prestin, SLC26A6, SlC26A7, and SLC26A9, localize to the surface membrane of transfected mammalian cells, we found exclusive lysosomal localization of SLC26A11. Renal collecting duct intercalated cells express SLC26A11 together with SLC26A4/pendrin and SLC26A7, and we therefore tested whether heterodimerization between these transporters might result in SLC26 transporter re-localization. Neither in HEK293T nor in immortalized intercalated cells co-expressing SLC26A11 with SLC26A4/pendrin or with SLC26A7, changes in SLC26A11 localization were observed. Moreover, native gel electrophoresis did not provide any evidence for heterodimerization of these isoforms. We next tested heterodimerization of SLC26A11 with SLC26A1, SLC26A2, SLC26A6, or SLC26A9 via co-expression in HEK293T cells and confocal imaging. For all combinations, no changes in subcellular distribution were observed. We conclude that SLC26A11 does not heterodimerize with other SLC26 proteins and that heterodimerization does not target SLC26A11 to cellular surface membranes.

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Section: Introductionmentioning

confidence: 99%

Oligomerization and cellular localization of SLC26A11

Bungert-Plümke,

Guzman,

Fahlke

2024

Preprint

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High albumen height by expression of GALNT9 and thin eggshell by decreased Ca2+ transportation caused high hatchability in Huainan partridge chicken

Yang,

Zhao,

Dou

et al. 2024

Poultry Science

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Chloride binding and cholesterol effects on high frequency complex nonlinear capacitance (cNLC) in the mouse outer hair cell: experiment and molecular dynamics

Bai,

Zhang,

Renigunta

et al. 2024

Preprint

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The function of prestin (SLC26a5), an anion transport family member, has evolved to enhance auditory sensitivity and frequency selectivity by providing mechanical feedback via outer hair cells (OHC) into the organ of Corti. The frequency extent of this boost is governed by the voltage-dependent kinetics of the protein charge movements, otherwise known as nonlinear capacitance (NLC) that we measure in membrane patches under voltage clamp. Here we extend our previous studies on guinea pig OHCs by studying the frequency response of NLC in the mouse OHC, a species with higher frequency auditory needs. We find that the characteristic frequency cut-off (Fis) for the mouse surpasses that of the guinea pig, being 27 kHz vs. 19 kHz, respectively; nevertheless, each shows significant activity in the ultrasonic range. We also evaluate the influence of anion binding on prestin frequency response. Several single point mutations within the chloride binding pocket of prestin (e.g., S396E, S398E) lack anion influence. In agreement, we show absence of anion binding through molecular dynamics (MD) simulations. NLC Fis in the S396E knock-in mouse remains the same as controls, indicating that high frequency activity is likely governed by viscoelastic loads within the membrane characterized by stretched-exponential frequency roll-off. Accordingly, treatment with MBCD, which removes membrane cholesterol, possibly from prestin itself, and can alter membrane fluidity, augments NLC Fis out to 39 kHz. Although interactions between membrane lipid and prestin have been suggested from structural studies to arise at their interfacial boundaries within the membrane, our MD simulations suggest that phospholipids can insert within transmembrane domains of prestin during voltage perturbation. Such novel lipid-protein interactions could account for our observed changes in the phase of prestin voltage-sensor charge movements across frequency. We hypothesize that because prestin tertiary structures of all species studied to-date are indistinguishable, it is likely that any special auditory requirements of individual species for cochlear amplification have evolved to capitalize on prestin performance by modifying, not the protein itself, but the external loads on the protein, including those within the membrane and organ of Corti.

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SLC26 Anion Transporters

Cited by 3 publications

References 279 publications

Oligomerization and cellular localization of SLC26A11

Oligomerization and cellular localization of SLC26A11

High albumen height by expression of GALNT9 and thin eggshell by decreased Ca2+ transportation caused high hatchability in Huainan partridge chicken

Chloride binding and cholesterol effects on high frequency complex nonlinear capacitance (cNLC) in the mouse outer hair cell: experiment and molecular dynamics

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