Journal
DEVELOPMENTAL CELL
Volume 12, Issue 1, Pages 129-141Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2006.10.015
Keywords
-
Categories
Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM036548, R01GM074241] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM074241, R01 GM036548, R01 GM036548-24, R01 GM074241, GM036548] Funding Source: Medline
Ask authors/readers for more resources
Upon activation by Wnt, the Frizzled receptor is internalized in a process that requires the recruitment of Dishevelled. We describe a novel interaction between Dishevelled2 (Dvl2) and mu 2-adaptin, a subunit of the clathrin adaptor AP-2; this interaction is required to engage activated Frizzled4 with the endocytic machinery and for its internalization. The interaction of Dvl2 with AP-2 requires simultaneous association of the DEP domain and a peptide YHEL motif within Dvl2 with the C terminus of mu 2. Dvl2 mutants in the YHEL motif fail to associate with mu 2 and AP-2, and prevent Frizzled4 internalization. Corresponding Xenopus Dishevelled mutants show compromised ability to interfere with gastrulation mediated by the planar cell polarity (PCP) pathway. Conversely, a Dvl2 mutant in its DEP domain impaired in PCP signaling exhibits defective AP-2 interaction and prevents the internalization of Frizzled4. We suggest that the direct interaction of Dvl2 with AP-2 is important for Frizzled internalization and Frizzled/PCP signaling.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available