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First published online March 21, 2007

Journal of Cell Science 120, 701e (2007)
© The Company of Biologists Limited
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In this issue

High FYVE for BMP signalling


Figure 1

Signalling by the transforming growth factor beta (TGFbeta) receptor superfamily involves second messengers called Smad proteins. These bind to the receptor complex, become phosphorylated and then translocate to the nucleus. The FYVE-domain protein SARA (Smad anchor for receptor activation) facilitates TGFbeta and activin/nodal signalling by recruiting unphosphorylated Smad2 and Smad3 to membranes. Now, Xu Cao and co-authors report that another FYVE-domain protein - endofin - acts as a Smad anchor during bone morphogenetic protein (BMP) signalling (see p. 1216). The authors show that endofin binds preferentially to Smad1 and enhances its phosphorylation and nuclear translocation upon BMP stimulation. RNAi studies indicate that endofin is required for BMP-dependent Smad1 phosphorylation. Furthermore, mutating the membrane-anchoring FYVE domain of endofin reduces BMP-responsive gene expression in cell cultures and Xenopus ectodermal explants. Finally, the authors show that endofin also recruits protein phosphatase 1, which dephosphorylates and inactivates the type 1 BMP receptor. Thus, they conclude, endofin both positively and negatively regulates BMP signalling.


Related articles in JCS:

Endofin acts as a Smad anchor for receptor activation in BMP signaling
Weibin Shi, Chenbei Chang, Shuyi Nie, Shutao Xie, Mei Wan, and Xu Cao
JCS 2007 120: 1216-1224. [Abstract] [Full Text]  




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