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Ubiquitination of Aquaporin-2 in the Kidney

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,...

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Detalles Bibliográficos
Autores principales: Lee, Yu-Jung, Kwon, Tae-Hwan
Formato: Texto
Lenguaje:English
Publicado: The Korean Society of Electrolyte Metabolism 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3041480/
https://www.ncbi.nlm.nih.gov/pubmed/21468177
http://dx.doi.org/10.5049/EBP.2009.7.1.1
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author Lee, Yu-Jung
Kwon, Tae-Hwan
author_facet Lee, Yu-Jung
Kwon, Tae-Hwan
author_sort Lee, Yu-Jung
collection PubMed
description 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.
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spelling pubmed-30414802011-04-05 Ubiquitination of Aquaporin-2 in the Kidney Lee, Yu-Jung Kwon, Tae-Hwan Electrolyte Blood Press Review Article 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. The Korean Society of Electrolyte Metabolism 2009-06 2009-06-30 /pmc/articles/PMC3041480/ /pubmed/21468177 http://dx.doi.org/10.5049/EBP.2009.7.1.1 Text en Copyright © 2009 The Korean Society of Electrolyte Metabolism http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Lee, Yu-Jung
Kwon, Tae-Hwan
Ubiquitination of Aquaporin-2 in the Kidney
title Ubiquitination of Aquaporin-2 in the Kidney
title_full Ubiquitination of Aquaporin-2 in the Kidney
title_fullStr Ubiquitination of Aquaporin-2 in the Kidney
title_full_unstemmed Ubiquitination of Aquaporin-2 in the Kidney
title_short Ubiquitination of Aquaporin-2 in the Kidney
title_sort ubiquitination of aquaporin-2 in the kidney
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3041480/
https://www.ncbi.nlm.nih.gov/pubmed/21468177
http://dx.doi.org/10.5049/EBP.2009.7.1.1
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