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Originally published In Press as doi:10.1074/jbc.M503511200 on June 23, 2005

J. Biol. Chem., Vol. 280, Issue 33, 29820-29827, August 19, 2005
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Repulsive Guidance Molecule (RGMa), a DRAGON Homologue, Is a Bone Morphogenetic Protein Co-receptor*

Jodie L. Babitt{ddagger}§, Ying Zhang{ddagger}§, Tarek A. Samad||, Yin Xia{ddagger}**, Jie Tang{ddagger}, Jason A. Campagna||, Alan L. Schneyer**, Clifford J. Woolf||, and Herbert Y. Lin{ddagger}{ddagger}{ddagger}

From the {ddagger}Program in Membrane Biology and Division of Nephrology, Department of Medicine, the ||Neural Plasticity Research Group, Department of Anesthesia and Critical Care, and the **Reproductive Endocrine Unit, Department of Medicine, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts 02129

Bone morphogenetic proteins (BMPs) are members of the transforming growth factor {beta} (TGF-{beta}) superfamily of ligands, which regulate many mammalian physiologic and pathophysiologic processes. BMPs exert their effects through type I and type II serine/threonine kinase receptors and the Smad intracellular signaling pathway. Recently, the glycosylphosphatidylinositol (GPI)-anchored protein DRAGON was identified as a co-receptor for BMP signaling. Here, we investigate whether a homologue of DRAGON, repulsive guidance molecule (RGMa), is similarly involved in the BMP signaling pathway. We show that RGMa enhances BMP, but not TGF-{beta}, signals in a ligand-dependent manner in cell culture. The soluble extracellular domain of RGMa fused to human Fc (RGMa.Fc) forms a complex with BMP type I receptors and binds directly and selectively to radiolabeled BMP-2 and BMP-4. RGMa mediates BMP signaling through the classical BMP signaling pathway involving Smad1, 5, and 8, and it up-regulates endogenous inhibitor of differentiation (Id1) protein, an important downstream target of BMP signals. Finally, we demonstrate that BMP signaling occurs in neurons that express RGMa in vivo. These data are consistent with a role for RGMa as a BMP co-receptor.

Received for publication, March 31, 2005 , and in revised form, June 10, 2005.

* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Both authors contributed equally to this work.

Supported in part by National Institutes of Health Grant F32 DK-068997.

{ddagger}{ddagger} Supported in part by National Institutes of Health Grants DK-57521 and DK-071837. To whom correspondence should be addressed: Program in Membrane Biology, 149 13th St., MGH-East CNY-8216, Charlestown, MA 02129. Tel.: 617-726-5661; Fax: 617-726-5669; E-mail: hlin{at}partners.org.


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