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

GSE279083 Mus musculus Expression profiling by high throughput sequencing 28 samples 2025/02/17 GPL19057
Summary
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).
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NCBI GEO page ↗ Paper (PMID 40062363) ↗ {# Names what the click gives you. "Open in finder" meant nothing to a visitor who arrived from a search engine and has never seen the tool. #} Find more mouse RNA-seq datasets →
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