scholarly journals Repulsive Guidance Molecule (RGMa), a DRAGON Homologue, Is a Bone Morphogenetic Protein Co-receptor

2005 ◽  
Vol 280 (33) ◽  
pp. 29820-29827 ◽  
Author(s):  
Jodie L. Babitt ◽  
Ying Zhang ◽  
Tarek A. Samad ◽  
Yin Xia ◽  
Jie Tang ◽  
...  
2007 ◽  
Vol 282 (25) ◽  
pp. 18129-18140 ◽  
Author(s):  
Yin Xia ◽  
Paul B. Yu ◽  
Yisrael Sidis ◽  
Hideyuki Beppu ◽  
Kenneth D. Bloch ◽  
...  

2015 ◽  
Vol 22 (6) ◽  
pp. 458-465 ◽  
Author(s):  
Eleanor G Healey ◽  
Benjamin Bishop ◽  
Jonathan Elegheert ◽  
Christian H Bell ◽  
Sergi Padilla-Parra ◽  
...  

Endocrinology ◽  
2005 ◽  
Vol 146 (8) ◽  
pp. 3614-3621 ◽  
Author(s):  
Yin Xia ◽  
Yisrael Sidis ◽  
Abir Mukherjee ◽  
Tarek A. Samad ◽  
Gary Brenner ◽  
...  

2008 ◽  
Vol 294 (4) ◽  
pp. C994-C1003 ◽  
Author(s):  
Robin Kuns-Hashimoto ◽  
David Kuninger ◽  
Mahta Nili ◽  
Peter Rotwein

Juvenile hemochromatosis is a severe and rapidly progressing hereditary disorder of iron overload, and it is caused primarily by defects in the gene encoding repulsive guidance molecule c/hemojuvelin (RGMc/HJV), a recently identified protein that undergoes a complicated biosynthetic pathway in muscle and liver, leading to cell membrane-linked single-chain and heterodimeric species, and two secreted single-chain isoforms. RGMc modulates expression of the hepatic iron regulatory factor, hepcidin, potentially through effects on signaling by the bone morphogenetic protein (BMP) family of soluble growth factors. To date, little is known about specific pathogenic defects in disease-causing RGMc/HJV proteins. Here we identify functional abnormalities in three juvenile hemochromatosis-linked mutants. Using a combination of approaches, we first show that BMP-2 could interact in biochemical assays with single-chain RGMc species, and also could bind to cell-associated RGMc. Two mouse RGMc amino acid substitution mutants, D165E and G313V (corresponding to human D172E and G320V), also could bind BMP-2, but less effectively than wild-type RGMc, while G92V (human G99V) could not. In contrast, the membrane-spanning protein, neogenin, a receptor for the related molecule, RGMa, preferentially bound membrane-associated heterodimeric RGMc and was able to interact on cells only with wild-type RGMc and G92V. Our results show that different isoforms of RGMc/HJV may play unique physiological roles through defined interactions with distinct signaling proteins and demonstrate that, in some disease-linked RGMc mutants, these interactions are defective.


2009 ◽  
Vol 47 (01) ◽  
Author(s):  
K Breitkopf ◽  
A Müller ◽  
L Ciuclan ◽  
E Wiercinska ◽  
P ten Dijke ◽  
...  

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