Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
J Cell Biol 2008 Sep 22;1826:1073-82. doi: 10.1083/jcb.200710188.
Show Gene links Show Anatomy links

Ryk cooperates with Frizzled 7 to promote Wnt11-mediated endocytosis and is essential for Xenopus laevis convergent extension movements.

Kim GH , Her JH , Han JK .

The single-pass transmembrane protein Ryk (atypical receptor related tyrosine kinase) functions as a Wnt receptor. However, Ryk''s correlation with Wnt/Frizzled (Fz) signaling is poorly understood. Here, we report that Ryk regulates Xenopus laevis convergent extension (CE) movements via the beta-arrestin 2 (betaarr2)-dependent endocytic process triggered by noncanonical Wnt signaling. During X. laevis gastrulation, betaarr2-mediated endocytosis of Fz7 and dishevelled (Dvl/Dsh) actually occurs in the dorsal marginal zone tissues, which actively participate in noncanonical Wnt signaling. Noncanonical Wnt11/Fz7-mediated endocytosis of Dsh requires the cell-membrane protein Ryk. Ryk interacts with both Wnt11 and betaarr2, cooperates with Fz7 to mediate Wnt11-stimulated endocytosis of Dsh, and signals the noncanonical Wnt pathway in CE movements. Conversely, depletion of Ryk and Wnt11 prevents Dsh endocytosis in dorsal marginal zone tissues. Our study suggests that Ryk functions as an essential regulator for noncanonical Wnt/Fz-mediated endocytosis in the regulation of X. laevis CE movements.

PubMed ID: 18809723
PMC ID: PMC2542470
Article link: J Cell Biol
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: arrb2 cfp chrd.1 dvl1 dvl2 fzd7 gsc mapk8 myc myod1 nodal3.2 odc1 pnkd rab5a rhoa ryk sia1 tbxt wnt11 wnt11b wnt5a
Morpholinos: arrb2 MO3 ryk MO1

Article Images: [+] show captions
References [+] :
Atfi, The disintegrin and metalloproteinase ADAM12 contributes to TGF-beta signaling through interaction with the type II receptor. 2007, Pubmed