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Dishevelled 2 recruits beta-arrestin 2 to mediate Wnt5A-stimulated endocytosis of Frizzled 4.

Science (New York, N.Y.) | Sep 5, 2003

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.

Pubmed ID: 12958364 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | Animals | Arrestins | Cell Line | Cell Membrane | Clathrin | Cytoplasm | Dishevelled Proteins | Drosophila Proteins | Endocytosis | Frizzled Receptors | Humans | Mice | Phosphoproteins | Phosphorylation | Protein Kinase C | Proteins | Proto-Oncogene Proteins | RNA, Small Interfering | Recombinant Fusion Proteins | Signal Transduction | Wnt Proteins | Wnt-5a Protein | beta-Arrestin 2 | beta-Arrestins

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Associated grants

  • Agency: NHLBI NIH HHS, Id: HL 16037
  • Agency: NHLBI NIH HHS, Id: HL 61365
  • Agency: NINDS NIH HHS, Id: NS 19576

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