![]() Overexpression of BMP-2 and BMP-4 alters the size and shape of developing skeletal elements in the chick limb. BMP/GDF-signalling interactions during synovial joint development. Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo. Signal relay by BMP antagonism controls the SHH/FGF4 feedback loop in vertebrate limb buds. The BMP antagonist Gremlin regulates outgrowth, chondrogenesis and programmed cell death in the developing limb. Control of vertebrate limb outgrowth by the proximal factor Meis2 and distal antagonism of BMPs by Gremlin. Morphogenesis of digits in the avian limb is controlled by FGFs, TGFβs, and noggin through BMP signaling. Endogenous and ectopic expression of noggin suggests a conserved mechanism for regulation of BMP function during limb and somite patterning. Identification of the ligand-binding site of the BMP type IA receptor for BMP-4. The cystine-knot growth-factor superfamily. DAN is a secreted glycoprotein related to Xenopus cerberus. Crystal structure of the BMP-2–BRIA ectodomain complex. BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II. Evolution and classification of cystine knot-containing hormones and related extracellular signaling molecules. Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor β superfamily. Novel approach to phasing proteins: derivatization by short cryo- soaking with halides. Biochemical and biophysical characterization of refolded Drosophila DPP, a homolog of bone morphogenetic proteins 2 and 4. Heparan sulfate proteoglycans retain Noggin at the cell surface: a potential mechanism for shaping bone morphogenetic protein gradients. Modified noggin polypeptide and compositions. Induction of a noggin-like gene by ectopic DV interaction during planarian regeneration. Noggin antagonizes BMP signalling to create a niche for adult neurogenesis. Mutations of the NOG gene in individuals with proximal symphalangism and multiple synostosis syndrome. Identical mutations in NOG can cause either tarsal/carpal coalition syndrome or proximal symphalangism. Heterozygous mutations in the gene encoding noggin affect human joint morphogenesis. Noggin, cartilage morphogenesis, and joint formation in the mammalian skeleton. The Spemann organizer signal noggin binds and inactivates bone morphogenetic protein 4. Dorsoventral patterning in Xenopus: inhibition of ventral signals by direct binding of chordin to BMP-4. The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities. ![]() Expression cloning of noggin, a new dorsalizing factor localized to the Spemann organizer in Xenopus embryos. Bone morphogenetic proteins: multifunctional regulators of vertebrate development. The scaffold of Noggin contains a cystine (the oxidized form of cysteine) knot topology similar to that of BMPs thus, ligand and antagonist seem to have evolved from a common ancestral gene. The BMP-7-binding affinity of site-specific variants of Noggin is correlated with alterations in bone formation and apoptosis in chick limb development, showing that Noggin functions by sequestering its ligand in an inactive complex. Here we report the crystal structure of the antagonist Noggin bound to BMP-7, which shows that Noggin inhibits BMP signalling by blocking the molecular interfaces of the binding epitopes for both type I and type II receptors. So far, the three-dimensional structures of BMP antagonists and the structural basis for inactivation have remained unknown. The interplay between bone morphogenetic proteins (BMPs) and their antagonists governs developmental and cellular processes as diverse as establishment of the embryonic dorsal–ventral axis, induction of neural tissue, formation of joints in the skeletal system and neurogenesis in the adult brain.
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