Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Sci. Signal., 9 September 2008
Vol. 1, Issue 36, p. ec319
[DOI: 10.1126/scisignal.136ec319]

EDITORS' CHOICE

Cell Biology Wnt Receptor Signaling

L. Bryan Ray

Science, Science Signaling, AAAS, Washington, DC 20005, USA

Wnt glycoproteins act as important signaling molecules in a range of processes from development to cancer. Pan et al. describe a missing link in the mechanism by which Wnt binding to its receptors initiates biochemical signaling within cells. They identified phosphatidylinositol-4-phosphate 5-kinase type I (PIP5KI) in a screen for components required for Wnt signaling in human cells. After activation, the Wnt receptor LRP6 becomes phosphorylated on serine and threonine residues, and PIP5KI was required for this event. The Wnt signaling component disheveled, a scaffold protein, interacted with PIP5KI, and disheveled and the Wnt receptor protein frizzled were required for Wnt-dependent formation of phosphatidylinositol 4,5-bisphosphate [PtdIns (4,5)P2]. Accumulation of PtdIns (4,5)P2 appeared to be necessary for the aggregation of LRP6 and its consequent phosphorylation.

W. Pan, S.-C. Choi, H. Wang, Y. Qin, L. Volpicelli-Daley, L. Swan, L. Lucast, C. Khoo, X. Zhang, L. Li, C. S. Abrams, S. Y. Sokol, D. Wu , Wnt3a-mediated formation of phosphatidylinositol 4,5-bisphosphate regulates LRP6 phosphorylation. Science 321, 1350-1353 (2008). [Abstract] [Full Text]

Citation: L. B. Ray, Wnt Receptor Signaling. Sci. Signal. 1, ec319 (2008).



To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882