+ |
WNK2 | up-regulates activity
phosphorylation
|
WNK1 |
0.56 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260790 |
Ser382 |
KRASFAKsVIGTPEF |
Homo sapiens |
|
pmid |
sentence |
22032326 |
WNK1, which is activated in response to osmotic stress by phosphorylation of its T-loop residue (Ser382). | We found that wild-type WNK2 (Figure 8A) or WNK3 (Figure 8B) phosphorylated kinase-inactive WNK1 (1–667, D368A) at Ser382 in vitro. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KLHL2 | down-regulates quantity by destabilization
binding
|
WNK2 |
0.452 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272120 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23838290 |
We found that KLHL2, as well as KLHL3, was co-immunoprecipitated with all four WNK isoforms. The direct interaction of KLHL2 with WNKs was confirmed on fluorescence correlation spectroscopy. Co-expression of KLHL2 and Cullin3 decreased the abundance of WNK1, WNK3 and WNK4 within HEK293T cells, and a significant increase of WNK4 ubiquitination by KLHL2 and Cullin3 was observed both in HEK293T cells and in an in vitro ubiquitination assay. These results suggest that KLHL2-Cullin3 also functions as an E3-ligase for WNK isoforms within the body. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Cullin 3-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
WNK2 |
0.301 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272125 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23838290 |
We found that KLHL2, as well as KLHL3, was co-immunoprecipitated with all four WNK isoforms. The direct interaction of KLHL2 with WNKs was confirmed on fluorescence correlation spectroscopy. Co-expression of KLHL2 and Cullin3 decreased the abundance of WNK1, WNK3 and WNK4 within HEK293T cells, and a significant increase of WNK4 ubiquitination by KLHL2 and Cullin3 was observed both in HEK293T cells and in an in vitro ubiquitination assay. These results suggest that KLHL2-Cullin3 also functions as an E3-ligase for WNK isoforms within the body. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |