scholarly journals Repulsive Guidance Molecule RGMa Alters Utilization of Bone Morphogenetic Protein (BMP) Type II Receptors by BMP2 and BMP4

2007 ◽  
Vol 282 (25) ◽  
pp. 18129-18140 ◽  
Author(s):  
Yin Xia ◽  
Paul B. Yu ◽  
Yisrael Sidis ◽  
Hideyuki Beppu ◽  
Kenneth D. Bloch ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Type Ii ◽  
Morphogenetic Protein ◽  
Repulsive Guidance Molecule ◽  
Guidance Molecule

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 ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Morphogenetic Protein ◽  
Repulsive Guidance Molecule ◽  
Guidance Molecule

scholarly journals Repulsive guidance molecule is a structural bridge between neogenin and bone morphogenetic protein

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

scholarly journals Localization and Action of Dragon (Repulsive Guidance Molecule b), a Novel Bone Morphogenetic Protein Coreceptor, throughout the Reproductive Axis

Endocrinology ◽  
2005 ◽  
Vol 146 (8) ◽  
pp. 3614-3621 ◽  
Author(s):  
Yin Xia ◽  
Yisrael Sidis ◽  
Abir Mukherjee ◽  
Tarek A. Samad ◽  
Gary Brenner ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Reproductive Axis ◽  
Morphogenetic Protein ◽  
Repulsive Guidance Molecule ◽  
Guidance Molecule

scholarly journals Identification of a Lysosomal Pathway Regulating Degradation of the Bone Morphogenetic Protein Receptor Type II

2010 ◽  
Vol 285 (48) ◽  
pp. 37641-37649 ◽  
Author(s):  
Hannah J. Durrington ◽  
Paul D. Upton ◽  
Simon Hoer ◽  
Jessica Boname ◽  
Benjamin J. Dunmore ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Receptor Type ◽  
Type Ii ◽  
Bone Morphogenetic Protein Receptor ◽  
Protein Receptor ◽  
Morphogenetic Protein

Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation

1999 ◽  
Vol 112 (20) ◽  
pp. 3519-3527 ◽  
Author(s):  
T. Ebisawa ◽  
K. Tada ◽  
I. Kitajima ◽  
K. Tojo ◽  
T.K. Sampath ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Osteoblast Differentiation ◽  
Transforming Growth Factor ◽  
C2c12 Cells ◽  
Nuclear Accumulation ◽  
Type I ◽  
Type Ii ◽  
Weakly Bound ◽  
Bmp Receptors ◽  
Morphogenetic Protein

Bone morphogenetic protein (BMP)-6 is a member of the transforming growth factor (TGF)-(β) superfamily, and is most similar to BMP-5, osteogenic protein (OP)-1/BMP-7, and OP-2/BMP-8. In the present study, we characterized the endogenous BMP-6 signaling pathway during osteoblast differentiation. BMP-6 strongly induced alkaline phosphatase (ALP) activity in cells of osteoblast lineage, including C2C12 cells, MC3T3-E1 cells, and ROB-C26 cells. The profile of binding of BMP-6 to type I and type II receptors was similar to that of OP-1/BMP-7 in C2C12 cells and MC3T3-E1 cells; BMP-6 strongly bound to activin receptor-like kinase (ALK)-2 (also termed ActR-I), together with type II receptors, i.e. BMP type II receptor (BMPR-II) and activin type II receptor (ActR-II). In addition, BMP-6 weakly bound to BMPR-IA (ALK-3), to which BMP-2 also bound. In contrast, binding of BMP-6 to BMPR-IB (ALK-6), and less efficiently to ALK-2 and BMPR-IA, together with BMPR-II was detected in ROB-C26 cells. Intracellular signalling was further studied using C2C12 and MC3T3-E1 cells. Among the receptor-regulated Smads activated by BMP receptors, BMP-6 strongly induced phosphorylation and nuclear accumulation of Smad5, and less efficiently those of Smad1. However, Smad8 was constitutively phosphorylated, and no further phosphorylation or nuclear accumulation of Smad8 by BMP-6 was observed. These findings indicate that in the process of differentiation to osteoblasts, BMP-6 binds to ALK-2 as well as other type I receptors, and transduces signals mainly through Smad5 and possibly through Smad1.

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