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EphA7 regulates claudin6 and pronephros development in Xenopus.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2018 Jan 08; Vol. 495 (2), pp. 1580-1587. Date of Electronic Publication: 2017 Dec 06. - Publication Year :
- 2018
-
Abstract
- Eph/ephrin molecules are widely expressed during embryonic development, and function in a variety of developmental processes. Here we studied the roles of the Eph receptor EphA7 and its soluble form in Xenopus pronephros development. EphA7 is specifically expressed in pronephric tubules at tadpole stages and knockdown of EphA7 by a translation blocking morpholino led to defects in tubule cell differentiation and morphogenesis. A soluble form of EphA7 (sEphA7) was also identified. Interestingly, the membrane level of claudin6 (CLDN6), a tetraspan transmembrane tight junction protein, was dramatically reduced in the translation blocking morpholino injected embryos, but not when a splicing morpholino was used, which blocks only the full length EphA7. In cultured cells, EphA7 binds and phosphorylates CLDN6, and reduces its distribution at the cell surface. Our work suggests a role of EphA7 in the regulation of cell adhesion during pronephros development, whereas sEphA7 works as an antagonist.<br /> (Copyright © 2017 Elsevier Inc. All rights reserved.)
- Subjects :
- Animals
Cell Membrane metabolism
Gene Expression Regulation, Developmental
Gene Knockdown Techniques
Oligodeoxyribonucleotides, Antisense genetics
Pronephros metabolism
Receptor, EphA7 antagonists & inhibitors
Receptor, EphA7 genetics
Solubility
Xenopus Proteins antagonists & inhibitors
Xenopus Proteins genetics
Xenopus laevis genetics
Claudins metabolism
Pronephros embryology
Receptor, EphA7 metabolism
Xenopus Proteins metabolism
Xenopus laevis embryology
Xenopus laevis metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 495
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 29223398
- Full Text :
- https://doi.org/10.1016/j.bbrc.2017.12.027