Interactions between Twist and other core epithelial–mesenchymal transition factors are controlled by GSK3-mediated phosphorylation
| Autor: | Talia Nasr, Rachel Lander, Carole LaBonne, Stacy D. Ochoa, Kara Nordin, Maneeshi S. Prasad |
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| Rok vydání: | 2013 |
| Předmět: |
Epithelial-Mesenchymal Transition
animal structures Blotting Western Molecular Sequence Data General Physics and Astronomy Plasma protein binding Xenopus Proteins Biology Article General Biochemistry Genetics and Molecular Biology Substrate Specificity Glycogen Synthase Kinase 3 Xenopus laevis Twist transcription factor Cell Movement GSK-3 Animals Immunoprecipitation Amino Acid Sequence Epithelial–mesenchymal transition Phosphorylation Twist Transcription factor In Situ Hybridization Body Patterning Multidisciplinary Protein Stability Twist-Related Protein 1 Gene Expression Regulation Developmental Neural crest General Chemistry Molecular biology Protein Structure Tertiary Cell biology Neural Crest Mutation Snail Family Transcription Factors Protein Binding Transcription Factors |
| Zdroj: | Nature Communications. 4 |
| ISSN: | 2041-1723 |
| Popis: | A subset of transcription factors classified as neural crest ‘specifiers’ are also core epithelial–mesenchymal transition regulatory factors, both in the neural crest and in tumour progression. The bHLH factor Twist is among the least well studied of these factors. Here we demonstrate that Twist is required for cranial neural crest formation and fate determination in Xenopus. We further show that Twist function in the neural crest is dependent upon its carboxy-terminal WR domain. The WR domain mediates physical interactions between Twist and other core epithelial–mesenchymal transition factors, including Snail1 and Snail2, which are essential for proper function. Interaction with Snail1/2, and Twist function more generally, is regulated by GSK-3-β-mediated phosphorylation of conserved sites in the WR domain. Together, these findings elucidate a mechanism for coordinated control of a group of structurally diverse factors that function as a regulatory unit in both developmental and pathological epithelial–mesenchymal transitions. |
| Databáze: | OpenAIRE |
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