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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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Formato: | Texto |
Lenguaje: | English |
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The Korean Society of Electrolyte Metabolism
2009
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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. |
format | Text |
id | pubmed-3041480 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | The Korean Society of Electrolyte Metabolism |
record_format | MEDLINE/PubMed |
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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