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First published online 15 November 2005
doi: 10.1242/jcs.02655

Journal of Cell Science 118, 5479-5487 (2005)
Published by The Company of Biologists 2005
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Research Article

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

Beatrice B. Yaroslavskiy1, Yongjun Zhang1, Sara E. Kalla1, Verónica García Palacios1, Allison C. Sharrow1, Yanan Li1, Mone Zaidi2, Chuanyue Wu1 and Harry C. Blair1,*

1 Departments of Pathology and of Cell Biology and Physiology, University of Pittsburgh and Veteran's Affairs Medical Center, Pittsburgh, PA 15243, USA
2 Mount Sinai Bone Program, Department of Medicine, Mount Sinai School of Medicine, New York, NY 10029, USA

* Author for correspondence (e-mail: hcblair{at}imap.pitt.edu)

Accepted 22 August 2005

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}vß3 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}vß3 ring in stationary cells, but alternating bands of VASP and {alpha}vß3 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}vß3 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.

Key words: Osteoclast, Nitric oxide, Cyclic GMP-dependent protein kinase I, Integrin, Vasodilator-stimulated phosphoprotein, Migfilin


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