Lysine acetylation of aquaporin-3 promotes water reabsorption but is not essential for urine concentration

The current study aimed to decipher the role of previously discovered K282 acetylation of aquaporin-3 (AQP3) in renal water homeostasis. C57BL/6J mice harboring amino acid subsitutions to model lysine acetylation (AQP3 K282Q, termed Q mutant) or deacetylation (AQP3 K282R, termed R mutant) and wild type (WT) controls were used to determine if these mutations affected the kidney transcriptome under ad libitum pelled chow and water (standard housing condictions). Male and female mice were included in the transcriptomic analyses, and all samples were collected between 8-11 am (Zeitgeber 2-5). Overall design: Wild Type (WT), acetylated mimetic (Q), and deacetylated mimetic (R), male and female mice were kept in standard housing conditions (pelleted food and tap water ad libitum; 12 h light: 12 h dark cycle). Mice were euthanized between ZT2-5 and kidneys excised, decapsulted, and snap frozen for RNA analyses.