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Electrolyte Blood Press. 2009 Jun;7(1):1-4. doi: 10.5049/EBP.2009.7.1.1. Epub 2009 Jun 30.

Ubiquitination of aquaporin-2 in the kidney.

Electrolyte & blood pressure : E & BP

Yu-Jung Lee, Tae-Hwan Kwon

Affiliations

  1. Department of Biochemistry and Cell Biology, School of Medicine, Kyungpook National University, Daegu, Korea.

PMID: 21468177 PMCID: PMC3041480 DOI: 10.5049/EBP.2009.7.1.1

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.

Keywords: aquaporin 2; kidney tubules, collecting; ubiquitination; vasopressins

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