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Título

Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II

AutorGuerrero-Esteo, Mercedes; Sánchez-Elsner, Tilman; Letamendía, Ainhoa; Bernabéu, Carmelo
Palabras claveHereditary hemorrhagic telangiectasia
Binding-protein endoglin
Human endothelial-cells
tgf-beta
Cellular-responses
Signaling receptors
Heart development
Expression
Phosphorylation
Betaglycan
Fecha de publicación9-ago-2002
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJ Biol Chem 277(32):29197-209 (2002)
ResumenEndoglin is an auxiliary component of the transforming growth factor-beta (TGF-beta) receptor system, able to associate with the signaling receptor types I (TbetaRI) and II (TbetaRII) in the presence of ligand and to modulate the cellular responses to TGF-beta1. Endoglin cannot bind ligand on its own but requires the presence of the signaling receptors, supporting a critical role for the interaction between endoglin and TbetaRI or TbetaRII. This study shows that full-length endoglin interacts with both TbetaRI and TbetaRII, independently of their kinase activation state or the presence of exogenous TGF-beta1. Truncated constructs encoding either the extracellular or the cytoplasmic domains of endoglin demonstrated that the association with the signaling receptors occurs through both extracellular and cytoplasmic domains. However, a more specific mapping revealed that the endoglin/TbetaRI interaction was different from that of endoglin/TbetaRII. TbetaRII interacts with the amino acid region 437-558 of the extracellular domain of endoglin, whereas TbetaRI interacts not only with the region 437-558 but also with the protein region located between amino acid 437 and the N terminus. Both TbetaRI and TbetaRII interact with the cytoplasmic domain of endoglin, but TbetaRI only interacts when the kinase domain is inactive, whereas TbetaRII remains associated in its active and inactive forms. Upon association, TbetaRI and TbetaRII phosphorylate the endoglin cytoplasmic domain, and then TbetaRI, but not TbetaRII, kinase dissociates from the complex. Conversely, endoglin expression results in an altered phosphorylation state of TbetaRII, TbetaRI, and downstream Smad proteins as well as a modulation of TGF-beta signaling, as measured by the reporter gene expression. These results suggest that by interacting through its extracellular and cytoplasmic domains with the signaling receptors, endoglin might affect TGF-beta responses.
Descripción14 p.-10 fig.
Versión del editorhttp://dx.doi.org/10.1074/jbc.M111991200
URIhttp://hdl.handle.net/10261/167807
DOI10.1074/jbc.M111991200
ISSN0021-9258
E-ISSN1083-351X
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