Kinases and G proteins join the Wnt receptor complex.
Wnt proteins form a family of secreted signaling proteins that play a key role in various developmental events such as cell differentiation, cell migration, cell polarity and cell proliferation. It is currently thought that Wnt proteins activate at least three different signaling pathways by binding to seven transmembrane receptors of the Frizzled family and the co-receptor LRP6. Despite our growing knowledge of intracellular components that mediate a Wnt signal, the molecular events at the membrane have remained rather unclear. Now several publications(1-4) indicate that Frizzled receptors are G-protein coupled and kinases were identified that phosphorylate the co-receptor LRP6. These data deepen our understanding of Wnt-mediated signal transduction and provide more insight into how specificity may be achieved.
Department of Biochemistry, University of Ulm, Germany.
Tom
T
Quaiser
Roman
R
Anton
Michael
M
Kühl
D000818:Animals; D020962:Heterotrimeric GTP-Binding Proteins / Q000378:metabolism*; D026502:LDL-Receptor Related Proteins / Q000378:metabolism; D010770:Phosphotransferases / Q000378:metabolism*; D011485:Protein Binding; D015398:Signal Transduction; D051153:Wnt Proteins / Q000378:metabolism*
D026502:LDL-Receptor Related Proteins; D051153:Wnt Proteins; D010770:Phosphotransferases; D020962:Heterotrimeric GTP-Binding Proteins