![]() ![]() N-RGMa shares the same binding site on the BMP ligand with the ectodomain of the BMP type I receptor A (BMP-R1A), meaning that RGM can induce the BMP canonical signaling pathway via activation of Smad 1/5/8. ![]() Notably, N-RGMa presents high affinity to bone morphogenetic proteins (BMP) ligands, making RGMa (and all the members of this family) a modulator of this important signaling pathway. However, RGMa signaling through integrins has not been reported thus far. The RGMa N-terminal domain (N-RGMa) harbours a signal peptide, an additional neogenin-binding site, and an RGD motif, that is known to be important in cell–cell adhesion processes mediated by integrins. This domain also harbours a von Willibrand type D structural domain, containing a GDPH autocatalytic site. The RGMa C-terminal domain (C-RGMa) harbours a GPI-anchor and presents affinity to the type I transmembrane neogenin receptor, which is known as a guidance receptor for migrating neuronal and mesodermal cells. These diverse functions can be performed by RGMa because it can signal through different receptors and work as a modular protein. It was originally identified as a repulsive clue in the orientation of axonal growth in the central and peripheral nervous system and as an important target for neuronal survival However, RGMa action domains were found to go beyond the processes related to neurogenesis and could be extended to different processes, including the induction of endochondral ossification during skeletal development, the suppression of endothelial tube formation, and inflammatory responses. Repulsive guidance molecule a (RGMa) comprises the first repulsive glycoprotein member identified in the family of repulsive guidance molecules. The Creative Commons Public Domain Dedication waiver ( ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. ![]()
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