Article
Decrease of WNK4 ubiquitination by disease-causing mutations of KLHL3 through different molecular mechanisms.
Biochemical and biophysical research communications - 13 Sept 2013
Mori Yutaro, Wakabayashi Mai, Mori Takayasu, Araki Yuya, Sohara Eisei, Rai Tatemitsu, Sasaki Sei, Uchida Shinichi
Abstract excerpt
Recently, we demonstrated that WNK4 is a substrate for KLHL3-Cullin3 (CUL3) E3 ubiquitin ligase complexes and that impaired WNK4 ubiquitination is a common mechanism for pseudohypoaldosteronism type II (PHAII) caused by WNK4, KLHL3, and CUL3 mutations. Among the various KLHL3 mutations that cause PHAII, we demonstrated that the R528H mutation in the Kelch domain decreased the binding to WNK4, thereby causing less...
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