PLAP-1/asporin inhibits activation of BMP receptor via its leucine-rich repeat motif

M. Tomoeda, S. Yamada, H. Shirai, Y. Ozawa, M. Yanagita, S. Murakami

Research output: Contribution to journalArticlepeer-review

41 Citations (Scopus)


We previously identified the novel gene, periodontal ligament-associated protein-1 (PLAP-1)/asporin and reported that PLAP-1/asporin inhibited bone morphogenetic protein-2 (BMP-2)-induced cytodifferentiation of periodontal ligament (PDL) cells probably by direct interaction with BMP-2. Here, we elucidated the detailed regulatory mechanism of this protein on BMP-2-induced cytodifferentiation of PDL cells. Recombinant PLAP-1/asporin inhibited BMP-2-induced cytodifferentiation of PDL cells and competitively prevented BMP-2 from binding to the BMP receptor-IB (BMPR-IB), resulting in inhibition of BMP-dependent activation of Smad proteins. The induction of mutation to the leucine-rich repeat (LRR) motif, especially LRR5, within PLAP-1/asporin rescued the inhibitory effect of PLAP-1/asporin on BMP-2. By contrast, a 26-amino acid peptide in the PLAP-1/asporin LRR5 sequence inhibited BMP-2 activity. Our findings indicate that PLAP-1/asporin inhibits BMP-2-induced differentiation of PDL cells resulting from inactivation of the BMP-2 signaling pathway and that LRR, especially LRR5 of PLAP-1/asporin, plays an important role in the PLAP-1/asporin-BMP-2 interaction.

Original languageEnglish
Pages (from-to)191-196
Number of pages6
JournalBiochemical and biophysical research communications
Issue number2
Publication statusPublished - 2008 Jun 27
Externally publishedYes


  • Asporin
  • BMP-2
  • Leucine-rich repeat
  • PLAP-1
  • SLRP
  • Smad

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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