Lyn inhibits osteoclast differentiation by interfering with PLCγ1-mediated Ca2+ signaling

Soo Hyun Yoon, Youngkyun Lee, Hyung Joon Kim, Zang Hee Lee, Seok Won Hyung, Sang Won Lee, Hong Hee Kim

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)


Osteoclasts differentiate from macrophage-lineage cells to become specialized for bone resorption function. By a proteomics approach, we found that Lyn was down-regulated by the osteoclast differentiation factor, receptor activator of NF-κB ligand (RANKL). The forced reduction of Lyn caused a striking increase in the RANKL-induced PLCγ1, Ca2+, and NFATc1 responses during differentiation. These data suggest that Lyn plays a negative role in osteoclastogenesis by interfering with the PLCγ1-mediated Ca2+ signaling that leads to NFATc1 activation. Consistent with the in vitro results, in vivo injection of Lyn specific siRNA into mice calvariae provoked a fulminant bone resorption. Our study provides the first evidence of the involvement of Lyn in the negative regulation of osteoclastogenesis by RANKL.

Original languageEnglish
Pages (from-to)1164-1170
Number of pages7
JournalFEBS Letters
Issue number7
Publication statusPublished - 2009 Apr 2

Bibliographical note

Funding Information:
This work was supported by 21C Frontier Functional Proteomics Project (FPR08B1-170), New Drug Target Discovery (M10748000257-07N4800-25710), and Science Research Center (R11-2008-023-01001-0) grants.


  • Lyn
  • Osteoclast

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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