de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Lypd6 Enhances Wnt/beta-Catenin Signaling by Promoting Lrp6 Phosphorylation in Raft Plasma Membrane Domains

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons15815

Schwille,  Petra
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Özhan, G., Sezgin, E., Wehner, D., Pfister, A. S., Kühl, S. J., Kagermeier-Schenk, B., et al. (2013). Lypd6 Enhances Wnt/beta-Catenin Signaling by Promoting Lrp6 Phosphorylation in Raft Plasma Membrane Domains. DEVELOPMENTAL CELL, 26(4), 331-345. doi:10.1016/j.devcel.2013.07.020.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-5B98-4
Abstract
Wnt/beta-catenin signaling plays critical roles during embryogenesis, tissue homeostasis, and regeneration. How Wnt-receptor complex activity is regulated is not yet fully understood. Here, we identify the Ly6 family protein LY6/PLAUR domain-containing 6 (Lypd6) as a positive feedback regulator of Wnt/beta-catenin signaling. lypd6 enhances Wnt signaling in zebrafish and Xenopus embryos and in mammalian cells, and it is required for wnt8-mediated patterning of the mesoderm and neuroectoderm during zebrafish gastrulation. Lypd6 is GPI anchored to the plasma membrane and physically interacts with the Wnt receptor Frizzled8 and the coreceptor Lrp6. Biophysical and biochemical evidence indicates that Lypd6 preferentially localizes to raft membrane domains, where Lrp6 is phosphorylated upon Wnt stimulation. lypd6 knockdown or mislocalization of the Lypd6 protein to nonraft membrane domains shifts Lrp6 phosphorylation to these domains and inhibits Wnt signaling. Thus, Lypd6 appears to control Lrp6 activation specifically in membrane rafts, which is essential for downstream signaling.