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J Biol Chem, Vol. 274, Issue 2, 584-594, January 8, 1999
Superfamily
,
From the Cancer and Blood Research Program, and
§ Program in Developmental Biology, Endoglin (CD105) is a transmembrane glycoprotein
that binds transforming growth factor (TGF)- Immunology and
¶ Medical Genetics and Microbiology,
1 and -3, and
coprecipitates with the Ser/Thr kinase signaling receptor complex by
affinity labeling of endothelial and leukemic cells. The present study shows that in addition to TGF-1 and -3, endoglin interacts with activin-A, bone morphogenetic protein (BMP)-7, and BMP-2 but requires coexpression of the respective ligand binding kinase receptor for this
association. Endoglin cannot bind ligands on its own and does not alter
binding to the kinase receptors. It binds TGF-1 and -3 by
associating with the TGF- type II receptor and interacts with
activin-A and BMP-7 via activin type II receptors, ActRII and ActRIIB,
regardless of which type I receptor partner is coexpressed. However,
endoglin binds BMP-2 by interacting with the ligand binding type I
receptors, ALK3 and ALK6. The formation of heteromeric signaling
complexes was not altered by the presence of endoglin, although it was
coprecipitated with these complexes. Endoglin did not interact with
BMP-7 through complexes containing the BMP type II receptor,
demonstrating specificity of its action. Our data suggest that endoglin
is an accessory protein of multiple kinase receptor complexes of the
TGF- superfamily.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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