Quick Search:

uzh logo
Browse by:

Zurich Open Repository and Archive

Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-6241

Verrey, F; Fakitsas, P; Adam, G; Staub, O (2008). Early transcriptional control of ENaC (de)ubiquitylation by aldosterone. Kidney International, 73(6):691-696.

[img] PDF - Registered users only
View at publisher
Accepted Version


Aldosterone increases sodium reabsorption across kidney target tubules already before it increases the number of transport proteins, indicating that the early functional response to aldosterone depends on the activation of preexisting channels and pumps. A central mediator of this action is the early aldosterone-induced kinase Sgk1 that de-represses the surface expression and activity of the epithelial sodium channel (ENaC). A main mechanism by which Sgk1 exerts this de-repression is the phosphorylation of the ubiquitin ligase Nedd4-2 that is thereby prevented from ubiquitylating ENaC. Among a series of new early aldosterone-induced gene products recently identified in kidney target tubules, an additional regulator of ENaC ubiquitylation, the deubiquitylating enzyme Usp2-45, was identified. Coexpression of Usp2-45 was shown to increase ENaC surface expression and activity, and to decrease its ubiquitylation in expression systems, whereas other Usps such as the splice variant Usp2-69 had no effect. Since both Sgk1 and Usp2-45 are similarly induced in distal colon as well, in contrast to other gene products strongly induced in kidney that are not regulated in colon, we suggest that (de)ubiquitylation is the major ENaC regulatory mechanism targeted by aldosterone in the short-term via transcriptional regulation.


37 citations in Web of Science®
41 citations in Scopus®
Google Scholar™



62 downloads since deposited on 10 Dec 2008
16 downloads since 12 months

Detailed statistics

Additional indexing

Item Type:Journal Article, refereed, further contribution
Communities & Collections:04 Faculty of Medicine > Center for Integrative Human Physiology
04 Faculty of Medicine > Institute of Physiology
07 Faculty of Science > Institute of Physiology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Date:March 2008
Deposited On:10 Dec 2008 07:51
Last Modified:05 Apr 2016 12:36
Publisher:Nature Publishing Group
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:10.1038/sj.ki.5002737
PubMed ID:18094676

Users (please log in): suggest update or correction for this item

Repository Staff Only: item control page