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Phosphorylation of serine residues S252, S268/S269, and S879 in p120 catenin activates migration of presomitic mesoderm in gastrulating zebrafish embryos

Dev Dyn. 2022-06; 
Ariana Kupai, Hiroko Nakahara, Kathleen M Voss, Matthew S Hirano, Alexis Rodriguez, Donna L Lackey, James F Murayama, Chase J Mathieson, Botao Shan, Emma C Horton, Grace H Curtis, Joyce Huang, Merrill B Hille
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Mutant Libraries … cell migration is reduced by the injection of the Sp-MO. Using co-injection of this SpMO with various … All DNA sequencing was performed by GenScript. All other mutants were ligated, … Get A Quote

摘要

background: Cadherin-associated protein p120 catenin regulates cell adhesion and migration in cell cultures and is required for axial elongation in embryos. Its roles in adhesion and cell migration are regulated by phosphorylation. We determined the effects of phosphorylation of six serine and three threonine residues in p120 catenin during zebrafish (Danio rerio) embryogenesis. results: We knocked down endogenous p120 catenin-δ1 with an antisense RNA-splice-site morpholino (Sp-MO) causing defects in axis elongation. These defects were rescued by co-injections of mRNAs for wildtype mouse p120 catenin-δ1-3A or various mutated forms. Several mRNAs containing serine or threonine codons singly or doubly mutated t... More

关键词

Cdc42 GTPase, Rac1 GTPase, VAV2, convergent extension, mesodermal cell migration, p120 catenin-δ1, serine-threonine phosphorylation