Interaction and functional interplay between endoglin and ALK-1, two components of the endothelial transforming growth factor-beta receptor complex.

Transforming growth factor-beta (TGF-beta) signaling in endothelial cells is able to modulate angiogenesis and vascular remodeling, although the underlying molecular mechanisms remain poorly understood. Endoglin and ALK-1 are components of the TGF-beta receptor complex, predominantly expressed in endothelial cells, and mutations in either endoglin or ALK-1 genes are responsible for ...
the vascular dysplasia known as hereditary hemorrhagic telangiectasia. Here we find that the extracellular and cytoplasmic domains of the auxiliary TGF-beta receptor endoglin interact with ALK-1 (a type I TGF-beta receptor). In addition, endoglin potentiates TGF-beta/ALK1 signaling, with the extracellular domain of endoglin contributing to this functional cooperation between endoglin and ALK-1. By contrast, endoglin appears to interfere with TGF-beta/ALK-5 signaling. These results suggest that the functional association of endoglin with ALK-1 is critical for the endothelial responses to TGF-beta.
Mesh Terms:
Activin Receptors, Type I, Activin Receptors, Type II, Animals, Antigens, CD, Cell Line, Cytoplasm, Drug Interactions, Endothelial Cells, Extracellular Space, Gene Expression Regulation, Humans, Inhibitor of Differentiation Protein 1, Promoter Regions, Genetic, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Receptors, Cell Surface, Receptors, Transforming Growth Factor beta, Repressor Proteins, Signal Transduction, Transcription Factors, Transfection, Vascular Cell Adhesion Molecule-1
J. Cell. Physiol.
Date: Aug. 01, 2005
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