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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
Author(s) -
Lee HyeKyung,
Park JongTae,
Cho YoungSik,
Bae HyunSook,
Cho MoonIl,
Park JooCheol
Publication year - 2012
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.24047
Subject(s) - ameloblast , phosphorylation , microbiology and biotechnology , bone morphogenetic protein , biology , biochemistry , enamel paint , materials science , composite material , gene
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: 1754–1765, 2012. © 2011 Wiley Periodicals, Inc.