Ubiquitination of Aquaporin: in the kidney.

Author: Yu Jung LEE ¹ ; Tae Hwan KWON
Author Information

1. Department of Biochemistry and Cell Biology, School of Medicine, Kyungpook National University, Daegu, Korea. thkwon@knu.ac.kr
Publication Type:Review
Keywords: kidney tubules, collecting; ubiquitination; vasopressins; aquaporin 2
MeSH: Aquaporin 2; Deamino Arginine Vasopressin; Endocytosis; Kidney; Kidney Tubules, Collecting; Ligases; Lysine; Proteins; Substrate Specificity; Ubiquitin; Ubiquitination; Vasopressins
From:Electrolytes & Blood Pressure 2009;7(1):1-4
CountryRepublic of Korea
Language:English
Abstract: Ubiquitination is known to be important for endocytosis and lysosomal degradation of aquaporin-2 (AQP2). Ubiquitin (Ub) is covalently attached to the lysine residue of the substrate proteins and activation and attachment of Ub to a target protein is mediated by the action of three enzymes (i.e., E1, E2, and E3). In particular, E3 Ub-protein ligases are known to have substrate specificity. This minireview will discuss the ubiquitination of AQP2 and identification of potential E3 Ub-protein ligases for 1-deamino-8-D-arginine vasopressin (dDAVP)-dependent AQP2 regulation.