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Papers In Press, published online ahead of print November 27, 2003
J. Biol. Chem, 10.1074/jbc.M311155200
Submitted on October 10, 2003
Revised on November 11, 2003
Accepted on November 27, 2003

Identification of Murr1 as a regulator of the human delta epithelial sodium channel

Wolfgang Biasio, Tina Chang, C. Joy McIntosh, and Fiona J. McDonald

Department of Physiology, University of Otago, Dunedin, Dunedin 9001

Corresponding Author: fiona.mcdonald{at}stonebow.otago.ac.nz

The human delta epithelial sodium channel (delta ENaC) subunit is related to the alpha , beta , and gamma ENaC subunits that control salt homeostasis. delta ENaC forms an amiloride-sensitive Na+ channel with the beta and gamma subunits. However, the in vivo function of delta ENaC is not known. To gain insight into the function of delta ENaC a yeast two hybrid screen of a human brain cDNA library was carried out using the C- and N-terminal domains of delta ENaC. A novel delta ENaC interactin g protein called Murr1 was isolated in the C-terminal domain screen. Murr1 is a 21 kDa protein mutated in Bedlington terriers suffering from copper toxicosis. The interaction of Murr1 and delta ENaC was confirmed by glutathione S-transferase pull down a s say and coimmunoprecipitation. To test the functional significance of the interaction, Murr1 was coexpressed with delta beta gamma ENaC in Xenopus oocytes. Murr1 inhibited amiloride-sensitive sodium current in a dose-dependent manner. In addition, dele tion of the last 59 amino acids of delta ENaC abolished the inhibition. Murr1 also bound to the beta and gamma ENaC subunits and inhibited alpha beta gamma ENaC sodium current. Therefore, these results suggest that Murr1 is a novel regulator of ENaC..p


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