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Literature summary for 3.4.19.12 extracted from

  • Butterworth, M.B.; Edinger, R.S.; Ovaa, H.; Burg, D.; Johnson, J.P.; Frizzell, R.A.
    The deubiquitinating enzyme UCH-L3 regulates the apical membrane recycling of the epithelial sodium channel (2007), J. Biol. Chem., 282, 37885-37893.
    View publication on PubMed
Search for more literature for 3.4.19.12

Application

Application Comment Organism
additional information dynamic regulation of apically located epithelial sodium channel by recycling, which is facilitated by UCH-L3 Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
4,5,6,7-tetrachloroindan-1,3-dione UCH-L3 inhibition reduces epithelial sodium channel currents, decreases apical membrane epithelial sodium channel expression and increases epithelial sodium channel ubiquitination at the apical surface Mus musculus
siRNA knockdown of UCH-L3 leads to a decrease of epithelial sodium channel currents Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
endosome
-
 Mus musculus 5768
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
collecting duct
-
 Mus musculus
-
epithelial cell UCH-L3 is the predominant deubiquitinating enzyme in endosomal compartments of collecting duct epithelial cells Mus musculus
-

Synonyms

Synonyms Comment Organism
ubiquitin C-terminal hydrolase isoform L3
-
 Mus musculus
UCH-L3
-
 Mus musculus