Ubiquitination of renal ENaC subunits in vivo.

ABSTRACT: Ubiquitination of the epithelial Na⁺ channel (ENaC) in epithelial cells may influence trafficking and hormonal regulation of the channels. We assessed ENaC ubiquitination (ub-ENaC) in mouse and rat kidneys using affinity beads to capture ubiquitinated proteins from tissue homogenates and Western blot analysis with anti-ENaC antibodies. Ub-αENaC was observed primarily as a series of proteins of apparent molecular mass of 40-70 kDa, consistent with the addition of variable numbers of ubiquitin molecules primarily to the NH₂-terminal cleaved fragment (~30 kDa) of the subunit. No significant Ub-βENaC was detected, indicating that ubiquitination of this subunit is minimal. For γENaC, the protein eluted from the affinity beads had the same apparent molecular mass as the cle

SUBMITTER: Frindt G 

PROVIDER: S-EPMC7294337 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature