Essential role for β-arrestin 2 in the regulation of Xenopus convergent extension movements

• Published in: The EMBO journal Vol. 26; no. 10; pp. 2513 - 2526
• Main Authors: Kim, Gun-Hwa, Han, Jin-Kwan
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 16.05.2007; Nature Publishing Group
• Subjects: Adaptor Proteins, Signal Transducing - chemistry; Adaptor Proteins, Signal Transducing - metabolism; Amino Acid Sequence; Animals; Arrestins - chemistry; Arrestins - genetics; Arrestins - metabolism; Arrestins - physiology; beta-Arrestins; Cell Movement - genetics; Cell Movement - physiology; Cell Polarity; Cloning, Molecular; convergent extension movements; Dishevelled Proteins; Embryo, Nonmammalian; Endocytosis; Fluorescent Antibody Technique, Direct; Gene Expression Regulation, Developmental; Immunoblotting; In Situ Hybridization; Molecular Sequence Data; Phosphoproteins - metabolism; planar cell polarity; rhoA GTP-Binding Protein - chemistry; rhoA GTP-Binding Protein - metabolism; RNA, Messenger - metabolism; Sequence Homology, Amino Acid; Signal Transduction; Tissue Distribution; Wnt pathway; Wnt Proteins - metabolism; Xenopus; Xenopus - embryology; Xenopus development; Xenopus Proteins - chemistry; Xenopus Proteins - metabolism; β-arrestin 2
• ISSN: 0261-4189; 1460-2075
• DOI: 10.1038/sj.emboj.7601688

β‐Arrestin 2 (βarr2) is a multifunctional protein that regulates numerous aspects of G‐protein‐coupled receptor function. However, its possible involvement in developmental processes is poorly understood. In this work, we examined the potential role of βarr2 during Xenopus early development. Gain‐ and loss‐of‐function studies showed that Xenopus βarr2 (xβarr2) is required for proper convergent extension (CE) movements, and normal cell polarization and intercalation without affecting cell fate. Moreover, for CE movements, βarr2 acts as an essential regulator of dishevelled‐mediated PCP (planar cell polarity) signaling, but not G‐protein‐mediated Ca2+ signaling. Notably, xβarr2 is localized with the same distribution as the dishevelled protein, which is reasonable, as xβarr2 is required for dishevelled activation of RhoA. Furthermore, xβarr2 interacts with the N‐terminal quarter of Daam1 and RhoA proteins, but not Rac1, and regulates RhoA activation through Daam1 activation for CE movements. We provide evidence that the endocytic activity of xβarr2 is essential for control of CE movements. Taken together, our results suggest that βarr2 has a pivotal role in the regulation of Xenopus CE movements.