論文 - 詳細
| RRC ID | 5609 |
|---|---|
| 著者 | Carreira-Barbosa F, Kajita M, Morel V, Wada H, Okamoto H, Martinez Arias A, Fujita Y, Wilson SW, Tada M. |
| タイトル | Flamingo regulates epiboly and convergence/extension movements through cell cohesive and signalling functions during zebrafish gastrulation. |
| ジャーナル | Development |
| Abstract |
During vertebrate gastrulation, the body axis is established by coordinated and directional movements of cells that include epiboly, involution, and convergence and extension (C&E). Recent work implicates a non-canonical Wnt/planar cell polarity (PCP) pathway in the regulation of C&E. The Drosophila atypical cadherin Flamingo (Fmi) and its vertebrate homologue Celsr, a 7-pass transmembrane protein with extracellular cadherin repeats, regulate several biological processes, including C&E, cochlear cell orientation, axonal pathfinding and neuronal migration. Fmi/Celsr can function together with molecules involved in PCP, such as Frizzled (Fz) and Dishevelled (Dsh), but there is also some evidence that it may act as a cell adhesion molecule in a PCP-pathway-independent manner. We show that abrogation of Celsr activity in zebrafish embryos results in epiboly defects that appear to be independent of the requirement for Celsr in PCP signalling during C&E. Using a C-terminal truncated form of Celsr that inhibits membrane presentation of wild-type Celsr through its putative pro-region, a hanging drop assay reveals that cells from embryos with compromised Celsr activity have different cohesive properties from wild-type cells. It is disruption of this ability of Celsr to affect cell cohesion that primarily leads to the in vivo epiboly defects. In addition, Lyn-Celsr, in which the intracellular domain of Celsr is fused to a membrane localisation signal (Lyn), inhibits Fz-Dsh complex formation during Wnt/PCP signalling without affecting epiboly. Fmi/Celsr therefore has a dual role in mediating two separate morphogenetic movements through its roles in mediating cell cohesion and Wnt/PCP signalling during zebrafish gastrulation. |
| 巻・号 | 136(3) |
| ページ | 383-92 |
| 公開日 | 2009-2-1 |
| DOI | 10.1242/dev.026542 |
| PII | dev.026542 |
| PMID | 19091770 |
| PMC | PMC2687588 |
| MeSH | Adaptor Proteins, Signal Transducing / metabolism Amino Acid Sequence Animals Body Patterning / physiology Cadherins / genetics Cadherins / physiology* Cell Adhesion / physiology Cell Line Cell Membrane / physiology Cell Movement / physiology* Cell Polarity / physiology Dishevelled Proteins Drosophila Proteins Embryo, Nonmammalian / physiology Frizzled Receptors / metabolism Gastrulation / physiology* Humans Molecular Sequence Data Phosphoproteins / metabolism Protein Multimerization Receptors, G-Protein-Coupled / metabolism Signal Transduction / physiology Zebrafish / embryology* Zebrafish / metabolism Zebrafish Proteins / genetics Zebrafish Proteins / metabolism Zebrafish Proteins / physiology* src-Family Kinases / metabolism |
| IF | 5.611 |
| 引用数 | 60 |
| WOS 分野 | DEVELOPMENTAL BIOLOGY |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 各媒体での言及数の合計 | 0 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| ゼブラフィッシュ | rw71 rw135 |