SLC26A11 Membrane Protein Introduction

Introduction of SLC26A11

SLC26A11, also known as solute carrier family 26 (anion exchanger) member 11, is an approximately 65.3 kDa transmembrane protein that consists of 606 amino acids. In humans, it is encoded by the SLC26A11 gene located on the chromosome 17q25.3. SLC26A11 is a newly identified chlorine channel, with an intracellular C terminus and an extracellular N terminus. It belongs to the solute carrier 26 (SLC26) family of anion transporters, featured by 3 characteristic motifs of the SLC26 sulfate/anion exchanger family. This protein contains 11 transmembrane domains and has an N-glycosylation site in the putative extracellular loop between transmembrane domains 7-8. SLC26A11 has shown abundant mRNA expression in the brain and kidney (2.9-kb transcript), and at lower levels in liver, lung, pancreas, heart, and skeletal muscle by northern blot analysis.

Function of SLC26A11 Membrane Protein

SLC26A11 is sensitive to the anion exchanger inhibitor 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS). SLC26A11 is a sodium-independent sulfate transporter like most SLC26A family members, which are significant for various cellular functions involving homeostasis and intracellular electrolyte balance. Moreover, it may cooperate with SLC26A2 to mediate DIDS-sensitive sulfate uptake in endothelial venules and endothelial cells. Databases searches indicated that SLC26A11 has 3 characteristic motifs of the SLC26 sulfate exchanger family, which is an SLC26 sulfate transporter signature, a sulfate transporter domain, as well as an anti-Sigma factor domain (STAS). Sequence alignments revealed that SLC26A11 shares 55% homology with yeast SUL2 and is the most different member in the human SLC26 family. Since it is more closely linked to sulfate transporters from yeast than other SLC26 family members. Mutations in human SLC26 genes are associated with several autosomal recessive disorders, while SLC26A11 mutations have been reported to be implicated in the deafness and autosomal dominant diseases.

Fig.1 A mechanism could be targeted to prevent and treat brain edema. (Neuronal swelling, the major cause of death in traumatic and ischemic brain injuries is initiated when aberrant entry of sodium ions and depolarization activates the voltage-gated chloride channel, SLC26A11). (Rungta, 2015)

Application of SLC26A11 Membrane Protein in Literature

1. Rahmati N., et al. SLC26A11 (KBAT) in purkinje cells is critical for inhibitory transmission and contributes to locomotor coordination. eNeuro. 2016, 3(3). PubMed ID: 27390771
   
   

   Both in vitro and in vivo purkinje cells (PCs) in L7-KBAT KOs revealed a significantly elevated action potential firing frequency of simple spikes, which was associated with impaired motor performance on the Erasmus Ladder. The findings supported a critical role for SLC26A11 in moderating chloride homeostasis and neuronal activity in cerebellums.

2. Hosoya M., et al. Overlapping expression of anion exchangers in the cochlea of a non-human primate suggests functional compensation. Neurosci Res. 2016, 110: 1-10. PubMed ID: 27091614
   
   

   Five transporters (SLC26A4, SLC26A6, SLC26A11 SLC4A2 and SLC4A3) were expressed within cells of the outer sulcus. The results exhibited a species-specific distribution pattern of anion exchangers in the cochlea, especially in the outer sulcus cells, suggesting a functional compensation on these exchangers.

3. Yuyama I., et al. Sulfur utilization of corals is enhanced by endosymbiotic algae. Biol Open. 2016, 5(9): 1299-1304. PubMed ID: 27493203
   
   

   The expression of a sulfur transporter (SLC26A11) in the previous study was upregulated in the presence of Symbiodinium cells in juveniles of the reef-building coral Acropora tenuis. In this study, autoradiography was performed by using (35)S-labeled sulfate ions to test the localization and the amount of incorporated radioactive sulfate in coral tissues and symbiotic algae.

4. Dijkstra K., et al. A biophysical model for cytotoxic cell swelling. J Neurosci. 2016, 36(47): 11881-11890. PubMed ID: 27881775
   
   

   This work presented a dynamic biophysical model comprised Hodgkin-Huxley-type ion currents, a recently discovered voltage-gated chloride flux via the ion exchanger SLC26A11, active KCC2-mediated chloride extrusion, together with ATP-dependent pumps.

5. Rungta R.L., et al. The cellular mechanisms of neuronal swelling underlying cytotoxic edema. Cell. 2015, 161(3): 610-621. PubMed ID: 25910210
   
   

   Pharmacological and siRNA-mediated knockdown screening determined that the ion exchanger SLC26A11 could surprisingly serve as a voltage-gated Cl(-) channel which was activated based on neuronal depolarization to membrane potentials lower than -20 mV. And blockade of SLC26A11 activity can attenuate both the neuronal swelling and cell death.

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Reference

1. Rungta R L, et al. (2015). The cellular mechanisms of neuronal swelling underlying cytotoxic edema. Cell. 161(3): 610-621.

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