Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 43, Issue 8, Pages 635-647Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2018.06.004
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Funding
- National Health and Medical Research Council (NHMRC) of Australia [GNT1103006, GNT1020755, GNT1099307]
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Protein modification by ubiquitination plays a key evolutionarily conserved role in regulating membrane proteins. Nedd4-2, a ubiquitin ligase, targets membrane proteins such as ion channels and transporters for ubiquitination. This Nedd4-2-mediated ubiquitination provides a crucial step in controlling the membrane availability of these proteins, thus affecting their signaling and physiological outcomes. In one well-studied example, Nedd4-2 fine-tunes the physiological function of the epithelial sodium channel (ENaC), thus modulating Na+ reabsorption by epithelia to maintain whole-body Na+ homeostasis. This review summarizes the key signaling pathways regulated by Nedd4-2 and the possible implications of such regulation in various pathologies.
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