March2 is required for head formation by mediating Dishevelled degradation in concert with Dapper1
| Autor: | Wonhee Han, Jin-Kwan Han, Sanguk Kim, Seong-Moon Cheong, Gun-Sik Cho, Jae-Seong Yang, Hyeyoon Lee, Youngmu Koo, Saet-Byeol Jo |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Scaffold protein chemistry.chemical_classification biology Xenopus Wnt signaling pathway Embryo biology.organism_classification Cell biology Ubiquitin ligase Dishevelled 03 medical and health sciences Cytosol 030104 developmental biology Ubiquitin chemistry biology.protein Molecular Biology Developmental Biology |
| Zdroj: | Development. |
| ISSN: | 1477-9129 0950-1991 |
| DOI: | 10.1242/dev.143107 |
| Popis: | Dishevelled (Dvl/Dsh) is a key scaffold protein that propagates Wnt signaling essential for embryogenesis and homeostasis. However, whether antagonism of Wnt signaling necessary for vertebrate head formation can be achieved through regulation of Dsh protein stability is unclear. Here we show that membrane-associated RING-CH2 (March2), a RING-type E3 ubiquitin ligase, antagonizes Wnt signaling by regulating the turnover of Dsh protein via ubiquitin-mediated lysosomal degradation in prospective head region of Xenopus. We further found that March2 acquires regional and functional specificities for head formation from the Dsh-interacting protein Dapper1 (Dpr1). Dpr1 stabilizes interaction between March2 and Dsh for mediating ubiquitination and subsequent degradation of Dsh protein only in the dorso-animal region of Xenopus embryo. These results suggest that March2 restricts cytosolic pools of Dsh protein and leads to subsequent limitation of Wnt signaling for the precise vertebrate head development. |
| Databáze: | OpenAIRE |
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