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We review the most recent data demonstrating that glycosylation and, in particular, phosphorylation and ubiquitination are mechanisms that regulate AQP2 activity, subcellular sorting and distribution, degradation, and protein interactions. From a clinical perspective, posttranslational modification resulting in protein misrouting or degradation may explain certain forms of nephrogenic diabetes insipidus. In addition to providing major insight into the function and dynamics of renal AQP2 regulation, the analysis of AQP2 posttranslational modification may provide general clues as to the role of posttranslational modification for regulation of other membrane proteins.<\/jats:p>","DOI":"10.1152\/ajprenal.00721.2010","type":"journal-article","created":{"date-parts":[[2011,2,10]],"date-time":"2011-02-10T02:10:40Z","timestamp":1297303840000},"page":"F1062-F1073","source":"Crossref","is-referenced-by-count":99,"title":["Regulation of the water channel aquaporin-2 by posttranslational modification"],"prefix":"10.1152","volume":"300","author":[{"given":"Hanne B.","family":"Moeller","sequence":"first","affiliation":[{"name":"The Water and Salt Research Center, Department of Anatomy, Aarhus University, Aarhus, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emma T. 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