Integrin-?3 mediates binding of Chordin to the cell surface and promotes its endocytosis

Larrain, J; BROWN C.; De Robertis E.M.

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.

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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