SLC26A8 is encoded by the SLC26A8 gene and is also known as Testis anion transporter 1, TAT1, Anion exchange transporter, and Solute carrier family 26 member 8. It belongs to the solute carrier 26 (SLC26) family, which is a transmembrane protein located at the plasma membrane of the cells and transporting a variety of monovalent and divalent anions, including chloride, bicarbonate, sulfate, and oxalate. SLC26A8 displays a SO42- transport activity at least partly through a SO42-/Cl- exchange mechanism.
|Basic Information of SLC26A8|
|Protein Name||Testis anion transporter 1|
|Aliases||Anion exchange transporter, Solute carrier family 26 member 8|
|Organism||Homo sapiens (Human)|
The functional studies performed so far indicate that SLC26A8 displays a SO42- transport activity at least partly through a SO42-/Cl- exchange mechanism. SLC26A8 transport activity toward the C2O42- but not the I- was also demonstrated. Deletion of SLC26A8 in the mouse was shown to induce a male sterility phenotype due to the lack of sperm motility and impaired capacitation but also to severe structural defects of the flagellum. SLC26A8 anion transport activity was essential for these processes and in human, SLC26A8 mutations could lead to male infertility. Meanwhile, physical interaction and co-localization of SLC26A8 and CFTR in the sperm is demonstrated by co-immunoprecipitation experiments in heterologous cells transiently transfected with plasmids encoding SLC26A8 and CFTR proteins. The interaction between CFTR and SLC26A8 might cooperate in both the sperm head and flagellum to regulate ion fluxes upon capacitation, which are required for the acrosomal reaction and the flagellum hyperactivation, respectively. Physical interaction of SLC26A8 with CFTR results in CFTR stimulation, which is involved in the regulation of the Cl- and/or HCO3- fluxes that are required to switch on the PKA-dependent downstream phosphorylation cascades during sperm motility and capacitation.
Fig.1 Model of the physical interaction between SLC26A8 and CFTR channel. (El, 2014)
This article focuses on the functional interaction of SLC26A8 with the CFTR channel. This article summarizes the newly published studies, which indicate the mutations in SLC26A8 are associated with a deregulation of the CFTR anion transport activity in the pathophysiological context of the sperm and the pulmonary cells. These findings in this article confirm the physiological relevance of SLC26 and CFTR cross-regulation, opening new gates for the treatment of cystic fibrosis.
This article reveals that SLC26A8 as a new family member (Slc26A8), very specifically expressed in male germ cells in both the human and the mouse. Meanwhile, SLC26A8 is essential for proper sperm tail differentiation and motility and is a critical component of the sperm annulus.
This article reports that the identification and characterization of heterozygous SLC26A8 missense mutations, which would abolish the functional interaction with the CFTR channel and potentially contribute to subfertility in men by impairing sperm motility and capacitation.
This article suggests that Tat1 (SLC26A8) is a novel sulfate transporter, which can interact with MgcRacGAP in spermatocytes specifically. These observations raise the possibility of a new regulatory pathway linking sulfate transport to Rho signaling in male germ cells.
The authors in this article apply mutational analysis in the coding region of the SLC26A8 gene in 83 male infertility patients and two groups of controls using single-strand conformational polymorphism and direct sequencing methods, and the results of this article suggest that the SLC26A8 mutations are not a common cause of male infertility.
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