PUBLICATION

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

Authors
Kupai, A., Nakahara, H., Voss, K.M., Hirano, M.S., Rodriguez, A., Lackey, D.L., Murayama, J.F., Mathieson, C.J., Shan, B., Horton, E.C., Curtis, G.H., Huang, J., Hille, M.B.
ID
ZDB-PUB-220622-14
Date
2022
Source
Developmental Dynamics : an official publication of the American Association of Anatomists   251(12): 1952-1967 (Journal)
Registered Authors
Hille, Merrill
Keywords
Cdc42 GTPase, Rac1 GTPase, VAV2, convergent extension, mesodermal cell migration, p120 catenin-δ1, serine-threonine phosphorylation
MeSH Terms
  • Animals
  • Cadherins/genetics
  • Cadherins/metabolism
  • Catenins/genetics
  • Catenins/metabolism
  • Glutamic Acid/metabolism
  • Mesoderm/metabolism
  • Mice
  • Phosphorylation
  • Serine*/metabolism
  • Threonine/metabolism
  • Zebrafish*/metabolism
PubMed
35706088 Full text @ Dev. Dyn.
Abstract
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.
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 to phosphomimetic glutamic acid rescued, and some non-phosphorylatable mutants did not.
We discovered that phosphorylation of serine residue S252 or S879 is required for convergent extension of zebrafish embryos, since rescue occurred only when these residues were mutated to glutamic acid. In addition, the phosphorylation of either S268 or S269 is required, not both, consistent with the presence of only a single one of these residues in two isoforms of zebrafish and Xenopus laevis. In summary, phosphorylation of multiple serine and threonine residues of p120 catenin activates migration of presomitic mesoderm of zebrafish embryos facilitating elongation of the dorsal axis. This article is protected by copyright. All rights reserved.
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