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Nedd 4 is an ubiquitous ligase which regulates the expression of the sodium epithelial channel, [[Enac|ENaC]]. Nedd4 binds to ENaC via WW-domains in the C terminal proline rich motifs of ENaC and mark the protein for ubiquination. [[ | Nedd 4 is an ubiquitous [[ligase|ligase]] which regulates the expression of the sodium epithelial channel, [[Enac|ENaC]]. Nedd4 binds to ENaC via [[WW-domains|WW-domains]] in the C terminal [[Proline|proline]] rich motifs of ENaC and mark the protein for [[ubiquination|ubiquination]]. [[Liddle Syndrome|Liddle’s syndrome causes]] a deletion of [[Amino_acids|amino acids]] in the C terminal of the beta or gamma subunits of ENaC, meaning that Nedd4 can no longer bind which leads to an increased expression of ENac, and [[Hypertension|hypertension]] <ref name="Fouladkou et al">Fouladkou,F., Alikhani-Koopaei,R., Vogt,B., Flores,S.Y.,Malbert-Colas,L.,Lecomte,M.C., Loffing,J., Frey,F.J., Frey,B.M. and Staub,O. "A naturally occurring human Nedd4-2 variant displays impaired ENaCregulation in Xenopus laevis oocytes" Am. J. Physiol. Renal Physiol. 287 (3), F550-F561 (2004)</ref>. | ||
=== References === | |||
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Latest revision as of 18:47, 13 November 2011
Nedd 4 is an ubiquitous ligase which regulates the expression of the sodium epithelial channel, ENaC. Nedd4 binds to ENaC via WW-domains in the C terminal proline rich motifs of ENaC and mark the protein for ubiquination. Liddle’s syndrome causes a deletion of amino acids in the C terminal of the beta or gamma subunits of ENaC, meaning that Nedd4 can no longer bind which leads to an increased expression of ENac, and hypertension [1].
References
- ↑ Fouladkou,F., Alikhani-Koopaei,R., Vogt,B., Flores,S.Y.,Malbert-Colas,L.,Lecomte,M.C., Loffing,J., Frey,F.J., Frey,B.M. and Staub,O. "A naturally occurring human Nedd4-2 variant displays impaired ENaCregulation in Xenopus laevis oocytes" Am. J. Physiol. Renal Physiol. 287 (3), F550-F561 (2004)