| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10762230 | Biochemical and Biophysical Research Communications | 2012 | 6 Pages |
Abstract
⺠WNK4 kinase domain isolated from Escherichia coli exhibits kinase activity. ⺠WNK4 phosphorylates mouse Na-Cl cotransporter NCC at Thr48 in vitro. ⺠Phospho-mimicking at Thr48 increases NCC abundance and Na+ uptake activity. ⺠In the presence of the acidic motif, Ca2+ regulates the kinase activity of WNK4. ⺠PHAII mutations in the acidic motif disrupt a Ca2+-sensing mechanism of WNK4.
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Authors
Tao Na, Guojin Wu, Ji-Bin Peng,