| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88882 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12050670 |
Dkk1 has been shown to inhibitwnt by binding to and antagonizing lrp5/6. Here we show that the transmembrane proteins kremen1 and kremen2 are high-affinity dkk1 receptors that functionally cooperate with dkk1 to blockwnt/beta-catenin . Kremen2 forms a ternary complex with dkk1 and lrp6, and induces rapid endocytosis and removal of thewntreceptor lrp6 from the plasma membranekremen2 forms a ternary complex with dkk1 and lrp6, and induces rapid endocytosis and removal of the wnt receptor lrp6 from the plasma membrane |
|
3.0
KREMEN2
- 
- 
binding
binding