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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

Cited 16 time in Web of Science Cited 17 time in Scopus
Authors

Lee, Hye-Kyung; Park, Jong-Tae; Cho, Young-Sik; Bae, Hyun-Sook; Cho, Moon-Il; Park, Joo-Cheol

Issue Date
2012-05
Publisher
John Wiley & Sons Inc.
Citation
Journal of Cellular Biochemistry, Vol.113 No.5, pp.1754-1765
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. J. Cell. Biochem. 113: 17541765, 2012. (C) 2011 Wiley Periodicals, Inc.
ISSN
0730-2312
URI
https://hdl.handle.net/10371/198638
DOI
https://doi.org/10.1002/jcb.24047
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