@article {cite-key,
	title = {Dishevelled 2 recruits beta-arrestin 2 to mediate Wnt5A-stimulated endocytosis of Frizzled 4.},
	journal = {Science},
	volume = {301},
	number = {5638},
	year = {2003},
	month = {Sep},
	pages = {1391{\textendash}1394},
	address = {Howard Hughes Medical Institute, Departments of Medicine and Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.},
	abstract = {Wnt proteins, regulators of development in many organisms, bind to seven transmembrane-spanning (7TMS) receptors called frizzleds, thereby recruiting the cytoplasmic molecule dishevelled (Dvl) to the plasma membrane.Frizzled-mediated endocytosis of Wg (a Drosophila Wnt protein) and lysosomal degradation may regulate the formation of morphogen gradients. Endocytosis of Frizzled 4 (Fz4) in human embryonic kidney 293 cells was dependent on added Wnt5A protein and was accomplished by the multifunctional adaptor protein beta-arrestin 2 (betaarr2), which was recruited to Fz4 by binding to phosphorylated Dvl2. These findings provide a previously unrecognized mechanism for receptor recruitment of beta-arrestin and demonstrate that Dvl plays an important role in the endocytosis of frizzled, as well as in promoting signaling.},
	issn = {1095-9203 (Electronic); 0036-8075 (Linking)},
	doi = {10.1126/science.1082808},
	author = {Chen, Wei and ten Berge, Derk and Brown, Jeff and Ahn, Seungkirl and Hu, Liaoyuan A and Miller, William E and Caron, Marc G and Barak, Larry S and Nusse, Roel and Lefkowitz, Robert J}
}
