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Kelch-like 3 and Cullin 3 regulate electrolyte homeostasis by means of ubiquitination and degradation of WNKShigeru Shibataa,b, Junhui Zhanga,b, Jeremy Puthumanaa,b, Kathryn L.Protease Inhibitor Cocktail Stonec, and Richard P.Rilotumumab Liftona,b,aDepartment of Genetics, bHoward Hughes Health-related Institute, and cW.PMID:27217159 M. Keck Facility, Yale University School of Medicine, New Haven, CTContributed by Richard P. Lifton, March 8, 2013 (sent for assessment February 25, 2013)Pseudohypoaldosteronism sort II (PHAII) is a rare Mendelian syndrome featuring hypertension and hyperkalemia resulting from constitutive renal salt reabsorption and impaired K+ secretion. Recently, mutations in Kelch-like 3 (KLHL3) and Cullin 3 (CUL3), elements of an E3 ubiquitin ligase complex, had been found to result in PHAII, suggesting that loss of this complex’s ability to target certain substrates for ubiquitination leads to PHAII. By MS and coimmunoprecipitation, we show that KLHL3 ordinarily binds to WNK1 and WNK4, members of WNK (with no lysine) kinase household which have previously been found mutated in PHAII. We show that this binding leads to ubiquitination, including polyubiquitination, of no less than 15 precise web pages in WNK4, result.