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JCS ePress online publication date 15 Nov 2005
doi: 10.1242/jcs.02655

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Research Article

NO-dependent osteoclast motility: reliance on cGMP-dependent protein kinase I and VASP


Beatrice B. Yaroslavskiy, Yongjun Zhang, Sara E. Kalla, Verónica García Palacios, Allison C. Sharrow, Yanan Li, Mone Zaidi, Chuanyue Wu, and Harry C. Blair*
* Author for correspondence (e-mail: hcblair{at}imap.pitt.edu)

The osteoclast degrades bone in cycles; between cycles, the cell is motile. Resorption occurs by acid transport into an extracellular compartment defined by an {alpha}v{beta}3 integrin ring. NO has been implicated in the regulation of bone turnover due to stretch or via estrogen signals, but a specific mechanism linking NO to osteoclastic activity has not been described. NO stimulates osteoclast motility, and at high concentrations NO causes detachment and terminates resorption. Here we demonstrate that NO regulates attachment through the cGMP-dependent protein kinase I (PKG I) via phosphorylation of the intermediate protein VASP. VASP colocalized with the {alpha}v{beta}3 ring in stationary cells, but alternating bands of VASP and {alpha}v{beta}3 occurred when motility was induced by NO donors or cGMP. Redistribution of VASP correlated with its phosphorylation. Dependency of NO-induced motility on PKG I and on VASP was shown by siRNA knockdown of each protein. VASP knockdown also altered distribution of {alpha}v{beta}3 at the attachment site. We conclude that PKG I and VASP are essential for reorganization of attachment and cytoplasmic proteins in motility induced by NO or by cGMP.
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