Tob proteins enhance inhibitory Smad-receptor interactions to repress BMP signaling.

50Citations
Citations of this article
32Readers
Mendeley users who have this article in their library.

Abstract

Tob inhibits bone morphogenetic protein (BMP) signaling by interacting with receptor-regulated Smads in osteoblasts. Here we provide evidence that Tob also interacts with the inhibitory Smads 6 and 7. A yeast two-hybrid screen identified Smad6 as a protein interacting with Tob. Tob co-localizes with Smad6 at the plasma membrane and enhances the interaction between Smad6 and activated BMP type I receptors. Furthermore, we have isolated Xenopus Tob2, and show that it cooperates with Smad6 in inducing secondary axes when expressed in early Xenopus embryos. Finally, Tob and Tob2 cooperate with Smad6 to inhibit endogenous BMP signaling in Xenopus embryonic explants and in cultured mammalian cells. Our results provide both in vitro and in vivo evidence that Tob inhibits endogenous BMP signaling by facilitating inhibitory Smad functions.

Cite

CITATION STYLE

APA

Yoshida, Y., von Bubnoff, A., Ikematsu, N., Blitz, I. L., Tsuzuku, J. K., Yoshida, E. H., … Cho, K. W. Y. (2003). Tob proteins enhance inhibitory Smad-receptor interactions to repress BMP signaling. Mechanisms of Development, 120(5), 629–637. https://doi.org/10.1016/S0925-4773(03)00020-0

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free