The close similarity between SLC9B2 protein and NhaA, its E. coli ortholog, which mediates electrogenic transport of these ions (Taglicht et al. 1993), suggested that SLC9B2 transport might likewise be electrogenic (Xiang et al. 2007). Later work, however, indicates that SLC9B2 mediates the exchange of a single metal ion for a single proton (Uzdavinys et al. 2017).
Mass spectroscopic studies suggest that SLC9B2 exists as a homodimer (Landreh et al. 2017).
Winkelmann, I, Ndi, M, Nji, E, von Ballmoos, C, Drew, D, Coinçon, M, Uzdavinys, P
Landreh, M, Gupta, K, Benesch, JL, Degiacomi, MT, Liko, I, Robinson, CV, Marklund, EG, Drew, D, Gault, J, Coinçon, M, Uzdavinys, P
Padan, E, Taglicht, D, Schuldiner, S
Muend, S, Xiang, M, Rao, R, Feng, M
Andersson, S, Bobulescu, IA, Fuster, DG, Shi, M, Zhang, J, Moe, OW
sodium:proton antiporter activity of SLC9B2 dimer [mitochondrial inner membrane]
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