Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus embryos.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 19492039.
- Also identified by DOI 10.1371/journal.pone.0005742 and PMC identifier 2683942.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The FLRT family of transmembrane proteins has been implicated in the regulation of FGF signalling, neurite outgrowth, homotypic cell sorting and cadherin-mediated adhesion. In an expression screen we identified the Netrin receptors Unc5B and Unc5D as high-affinity FLRT3 interactors. Upon overexpression, Unc5B phenocopies FLRT3 and both proteins synergize in inducing cell deadhesion in Xenopus embryos. Morpholino knock-downs of Unc5B and FLRT3 synergistically affect Xenopus development and induce morphogenetic defects. The small GTPase Rnd1, which transmits FLRT3 deadhesion activity, physically and functionally interacts with Unc5B, and mediates its effect on cell adhesion. The results suggest that FLRT3, Unc5B and Rnd1 proteins interact to modulate cell adhesion in early Xenopus development.
Medical subject headings
- Embryo, Nonmammalian
- Membrane Proteins
- Receptors, Cell Surface
- Xenopus
- Xenopus Proteins
- rho GTP-Binding Proteins