| First Author | Ohsugi M | Year | 1999 |
| Journal | Dev Dyn | Volume | 216 |
| Issue | 2 | Pages | 168-76 |
| PubMed ID | 10536056 | Mgi Jnum | J:57953 |
| Mgi Id | MGI:1346239 | Doi | 10.1002/(SICI)1097-0177(199910)216:2<168::AID-DVDY7>3.0.CO;2-R |
| Citation | Ohsugi M, et al. (1999) Beta-catenin is a major tyrosine-phosphorylated protein during mouse oocyte maturation and preimplantation development. Dev Dyn 216(2):168-76 |
| abstractText | During mouse preimplantation development, the components of the E-cadherin-catenin complex are derived from both maternal and zygotic gene activity and the adhesion complex is increasingly accumulated and stored in a nonfunctional form, ready to be used for compaction and the formation of the trophectoderm cell layer (Ohsugi et al., Dev. Dyn. 206:391-402, 1996). Here, we show that beta-catenin is a major tyrosine-phosphorylated protein in oocytes and early cleavage-stage embryos and that the relative amount of phosphorylated beta-catenin is greatly reduced during the morula-blastocyst transition. Peptide-specific antibodies indicate that beta-catenin undergoes conformational changes and/or that the carboxy-terminal region of beta-catenin is blocked during preimplantation development. Moreover, the availability of a carboxy-terminal epitope seems to depend on the tyrosine phosphorylation state of beta-catenin and becomes unmasked when oocytes are treated with the tyrosine kinase inhibitor genistein. Our results suggest that tyrosine phosphorylation of beta-catenin represents a molecular mechanism to keep the accumulating E-cadherin adhesion complex in a nonfunctional form. Dev Dyn 1999;216:168-176. Copyright 1999 Wiley-Liss, Inc. |
