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A new signaling pathway that is involved in the BMP signaling
Author(s) -
Hagihara Meiko,
Yamashita Toshihide
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.530.3
Subject(s) - bone morphogenetic protein , microbiology and biotechnology , osteoblast , bmpr2 , bone morphogenetic protein 10 , signal transduction , chemistry , phosphorylation , bone morphogenetic protein 2 , bone morphogenetic protein 7 , biology , biochemistry , gene , in vitro
Bone morphogenetic proteins (BMPs) are multifunctional proteins that comprise the largest subfamily of the transforming growth factors‐beta. BMPs transduce the signal through BMP type I and type II receptors. Here we identify a new protein that directly binds to BMPs. This protein has a transmembrane domain that localizes at the plasma membrane. Although BMP‐2 as well as BMP‐4 induces osteoblast differentiation of ST2 cells, knockdown of this protein results in suppression of the osteoblast differentiation and phosphorylation of smad1/5/8 induced by BMPs, suggesting that the protein enhances the BMPs signals. The osteoblast differentiation maintained by BMPs binding to the protein appears to be dependent on the activity of RhoA. Thus, we uncover a new mechanism that regulates the signaling pathway from BMPs to smads and osteoblast differentiation.