SMOC-1 interacts with both BMP and glypican to regulate BMP signaling.

Secreted modular calcium binding (SMOC) proteins are conserved matricellular proteins found in organisms from to humans. SMOC homologs characteristically contain one or two extracellular calcium (EC) binding domain(s) and one or two thyroglobulin type-1 (TY) domain(s). SMOC proteins in and Xenopus have been found to interact with cell surface heparan sulfate protein glycans (HSPGs) to exert both positive and negative influences on the conserved bone morphogenetic protein (BMP) signaling pathway.

GPN-1/glypican and UNC-52/perlecan do not appear to function in BMP signaling to pattern the postembryonic mesoderm.

Heparan sulfate proteoglycans (HSPGs) are diverse macromolecules consisting of a protein core modified with glycosaminoglycan (GAG) chains. HSPGs, including glypicans and perlecans, have been implicated in shaping the extracellular matrix (ECM) to affect growth factor signaling. Here, we tested if GPN-1/glypicanor UNC-52/perlecan plays a role in the bone morphogenetic protein (BMP) signaling pathway in patterning the postembryonic mesoderm.

The SMOC-1 Protein Acts Cell Nonautonomously To Promote Bone Morphogenetic Protein Signaling.

Bone morphogenetic protein (BMP) signaling regulates many different developmental and homeostatic processes in metazoans. The BMP pathway is conserved in , and is known to regulate body size and mesoderm development. We have identified the (Secreted MOdular Calcium-binding protein-1) gene as a new player in the BMP pathway.