The evolutionarily conserved BMP-binding protein Twisted gastrulation promotes BMP signalling

• Published in: Nature (London) Vol. 405; no. 6788; pp. 757 - 763
• Main Authors: De Robertis, Eddy M, Oelgeschläger, Michael, Larraín, Juan, Geissert, Douglas
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 15.06.2000
• Subjects: Amino Acid Sequence; Animals; Binding, Competitive; Biological Evolution; Body Patterning - physiology; Bone Morphogenetic Protein 4; Bone Morphogenetic Proteins - metabolism; Cell Line; Chd/Sog protein; Conserved Sequence; Drosophila; Drosophila Proteins; Embryos; Evolution; gastrulation; Glycoproteins - antagonists & inhibitors; Glycoproteins - metabolism; Humans; Intercellular Signaling Peptides and Proteins; Molecular Sequence Data; Protein Binding; Proteins; Proteins - genetics; Proteins - metabolism; Signal Transduction; Space life sciences; Tsg protein; Vertebrates; Xenopus; Xenopus Proteins
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/35015500

Dorsal-ventral patterning in vertebrate and Drosophila embryos requires a conserved system of extracellular proteins to generate a positional information gradient. The components involved include bone morphogenetic proteins (BMP/Dpp), a BMP antagonist (Chordin/Short gastrulation; Chd/Sog) and a secreted metalloproteinase (Xolloid/Tolloid) that cleaves Chd/Sog. Here we describe Xenopus Twisted gastrulation (xTsg), another member of this signalling pathway. xTsg is expressed ventrally as part of the BMP-4 synexpression group and encodes a secreted BMP-binding protein that is a BMP signalling agonist. The data suggest a molecular mechanism by which xTsg dislodges latent BMPs bound to Chordin BMP-binding fragments generated by Xolloid cleavage, providing a permissive signal that allows high BMP signalling in the embryo. Drosophila Tsg also binds BMPs and is expressed dorsally, supporting the proposal that the dorsal-ventral axis was inverted in the course of animal evolution.