Twisted is a conserved extracellular BMP antagonist

Jeffrey J. Ross, Osamu Shimmi, Peter Vilmos, Anna Petryk, Hyon Kim, Karin Gaudenz, Spencer Hermanson, Stephen C. Ekker, Michael B. O'connor, J. Lawrence Marsh

Research output: Contribution to journalArticlepeer-review

230 Scopus citations


Bone morphogenetic protein (BMP) signalling regulates embryonic dorsal-ventral cell fate decisions in flies, frogs and fish 1. BMP activity is controlled by several secreted factors including the antagonists chordin and short gastrulation (SOG) 2,3. Here we show that a second secreted protein, Twisted gastrulation (Tsg) 4, enhances the antagonistic activity of Sog/chordin. In Drosophila, visualization of BMP signalling using anti-phospho-Smad staining 5 shows that the tsg and sog loss-of-function phenotypes are very similar. In S2 cells and imaginal discs, TSG and SOG together make a more effective inhibitor of BMP signalling than either of them alone. Blocking Tsg function in zebrafish with morpholino oligonucleotides causes ventralization similar to that produced by chordin mutants. Co-injection of sub-inhibitory levels of morpholines directed against both Tsg and chordin synergistically enhances the penetrance of the ventralized phenotype. We show that Tsgs from different species are functionally equivalent, and conclude that Tsg is a conserved protein that functions with SOG/chordin to antagonize BMP signalling.

Original languageEnglish (US)
Pages (from-to)479-483
Number of pages5
Issue number6827
StatePublished - Mar 22 2001

ASJC Scopus subject areas

  • General


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