DAP12 couples c-Fms activation to the osteoclast cytoskeleton by recruitment of Syk.
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ABSTRACT:
SUBMITTER: Zou W
PROVIDER: S-EPMC2584874 | biostudies-other | 2008 Aug
REPOSITORIES: biostudies-other
Publications
DAP12 couples c-Fms activation to the osteoclast cytoskeleton by recruitment of Syk.
Zou Wei W Reeve Jennifer L JL Liu Yuli Y Teitelbaum Steven L SL Ross F Patrick FP
Molecular cell 20080801 3
We examined the mechanism by which M-CSF regulates the cytoskeleton and function of the osteoclast, the exclusive bone resorptive cell. We show that binding of M-CSF to its receptor c-Fms generates a signaling complex comprising phosphorylated DAP12, an adaptor containing an immunoreceptor tyrosine-based activation motif (ITAM) and the nonreceptor tyrosine kinase Syk. c-Fms tyrosine 559, the exclusive binding site of c-Src, is necessary for regulation of DAP12/Syk signaling. Deletion of either o ...[more]
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