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1: EMBO Rep. 2003 Aug;4(8):813-8. Epub 2003 Jul 25.
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Integrin-alpha3 mediates binding of Chordin to the cell surface and promotes its endocytosis.

Larraín J, Brown C, De Robertis EM.

Howard Hughes Medical Institute, Department of Biological Chemistry, University of California, Los Angeles 90095-1662, USA.

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-alpha3. Integrin-alpha3 and Chd are co-expressed in the Xenopus embryo. Transfection of Integrin-alpha3 increased the binding of Chd to the cell surface, which was competed by an excess of soluble Integrin-alpha3. After binding to the cell surface, Chd was translocated into intracellular endocytic compartments in a temperature-dependent manner. We propose that Integrin-alpha3 may regulate the concentration of Chd protein in the extracellular space by endocytosis.

Publication Types:
PMID: 12897802 [PubMed - indexed for MEDLINE]

PMCID: PMC1326342