Publication: C-terminally truncated, kidney-specific variants of the WNK4 kinase lack several sites that regulate its activity
C-terminally truncated, kidney-specific variants of the WNK4 kinase lack several sites that regulate its activity
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Murillo-de-Ozores, A. R., Rodríguez-Gama, A., Bazúa-Valenti, S., Leyva-Ríos, K., Vázquez, N., Pacheco-Álvarez, D., De La Rosa-Velázquez, I. A., Wengi, A., Stone, K. L., Zhang, J., Loffing, J., Lifton, R. P., Yang, C.-L., Ellison, D. H., Gamba, G., & Castañeda-Bueno, M. (2018). C-terminally truncated, kidney-specific variants of the WNK4 kinase lack several sites that regulate its activity. Journal of Biological Chemistry, 293(31), 12209–12221. https://doi.org/10.1074/jbc.RA118.003037
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WNK lysine-deficient protein kinase 4 (WNK4) is an important regulator of renal salt handling. Mutations in its gene cause pseudohypoaldosteronism type II, mainly arising from overactivation of the renal Na+/Cl- cotransporter (NCC). In addition to full-length WNK4, we have observed faster migrating bands (between 95 and 130 kDa) in Western blots of kidney lysates. Therefore, we hypothesized that these could correspond to uncharacterized WNK4 variants. Here, using several WNK4 antibodies and WNK4-/- mice as controls, we showed that the
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Murillo-de-Ozores, A. R., Rodríguez-Gama, A., Bazúa-Valenti, S., Leyva-Ríos, K., Vázquez, N., Pacheco-Álvarez, D., De La Rosa-Velázquez, I. A., Wengi, A., Stone, K. L., Zhang, J., Loffing, J., Lifton, R. P., Yang, C.-L., Ellison, D. H., Gamba, G., & Castañeda-Bueno, M. (2018). C-terminally truncated, kidney-specific variants of the WNK4 kinase lack several sites that regulate its activity. Journal of Biological Chemistry, 293(31), 12209–12221. https://doi.org/10.1074/jbc.RA118.003037