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Odontogenic ameloblasts-associated protein (ODAM), via phosphorylation by bone morphogenetic protein receptor type IB (BMPR-IB), is implicated in ameloblast differentiation

Authors
 Hye-Kyung Lee  ;  Jong-Tae Park  ;  Young-Sik Cho  ;  Hyun-Sook Bae  ;  Moon-Il Cho  ;  Joo-Cheol Park 
Citation
 Journal of Cellular Biochemistry, Vol.113(5) : 1754-1765, 2012 
Journal Title
 Journal of Cellular Biochemistry 
ISSN
 0730-2312 
Issue Date
2012
Abstract
To elucidate the function of the odontogenic ameloblast-associated protein (ODAM) in ameloblasts, we identified more than 74 proteins that interact with ODAM using protoarray. Of the identified proteins, bone morphogenetic protein receptor type-IB (BMPR-IB) was physiologically relevant in differentiating ameloblasts. ODAM and BMPR-IB exhibited similar patterns of expression in vitro, during ameloblast differentiation. ODAM and BMPR-IB interacted through the C-terminus of ODAM, which resulted in increased ODAM phosphorylation in the presence of bone morphogenetic protein 2 (BMP-2). Immunoprecipitation assays using Ser-Xaa-Glu (SXE) mutants of ODAM demonstrated that the phosphorylation of ODAM by BMPR-IB occurs at this motif, and this phosphorylation is required for the activation of MAPKs. ODAM phosphorylation was detected in ameloblasts during ameloblast differentiation and enamel mineralization in vitro and involved in the activation of downstream factors of MAPKs. Therefore, the BMP-2-BMPR-IB-ODAM-MAPK signaling cascade has important roles in ameloblast differentiation and enamel mineralization. Our data suggest that ODAM facilitates the progression of tooth development in cooperation with BMPR-IB through distinct domains of ODAM.
Full Text
http://onlinelibrary.wiley.com/doi/10.1002/jcb.24047/abstract
DOI
10.1002/jcb.24047
Appears in Collections:
5. Research Institutes (연구소) > Human Identification Research Center (개인식별연구소) > 1. Journal Papers
Yonsei Authors
박종태(Park, Jong Tae)
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URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/90668
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