Integrin-?3 mediates binding of Chordin to the cell surface and promotes its endocytosis
Keywords: temperature, conservation, mouse, development, endocytosis, expression, binding, protein, cell, gene, dependence, space, drosophila, mechanism, embryo, line, surface, transduction, morphogenesis, strain, xenopus, pattern, signal, formation, bone, affinity, drug, vertebrate, translocation, integrin, article, analysis, endosome, genetic, concentration, transfection, chordin, controlled, observation, animal, study, priority, nonhuman, journal, Animalia, intracellular, Vertebrata, unclassified, extracellular, regulatory, morphogenetic, (parameters), COS7, alpha3
Abstract
Dorsoventral patterning in animal development is regulated by a morphogenetic gradient of Bone morphogenetic protein signalling, which is established by a set of proteins that are conserved from Drosophila to vertebrates. These include Chordin (Chd)/Short gastrulation, Xolloid/Tolloid and Twisted gastrulation. Here, we report the identification of a cell-surface component of this morphogenetic pathway. Prompted by the observation that Chd protein bound to the surface of certain cell lines with subnanomolar affinity, we identified two cell-surface proteins that bind to Chd, one of which corresponds to Integrin-?3. Integrin-?3 and Chd are co-expressed in the Xenopus embryo. Transfection of Integrin-?3 increased the binding of Chd to the cell surface, which was competed by an excess of soluble Integrin-?3. After binding to the cell surface, Chd was translocated into intracellular endocytic compartments in a temperature-dependent manner. We propose that Integrin-?3 may regulate the concentration of Chd protein in the extracellular space by endocytosis.
Más información
Título según SCOPUS: | Integrin-?3 mediates binding of Chordin to the cell surface and promotes its endocytosis |
Título de la Revista: | EMBO REPORTS |
Volumen: | 4 |
Número: | 8 |
Editorial: | Wiley |
Fecha de publicación: | 2003 |
Página de inicio: | 813 |
Página final: | 818 |
Idioma: | English |
URL: | http://www.scopus.com/inward/record.url?eid=2-s2.0-0042854717&partnerID=q2rCbXpz |
DOI: |
10.1038/sj.embor.embor902 |
Notas: | SCOPUS |