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Kinases and G proteins join the Wnt receptor complex
Author(s) -
Quaiser Tom,
Anton Roman,
Kühl Michael
Publication year - 2006
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.20386
Subject(s) - frizzled , wnt signaling pathway , lrp6 , microbiology and biotechnology , signal transduction , biology , receptor , transmembrane protein , cell surface receptor , lrp5 , kinase , intracellular , biochemistry
Abstract 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 publications1–4 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. BioEssays 28: 339–343, 2006. © 2006 Wiley Periodicals, Inc.