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MBC in Press, published online ahead of print May 4, 2005
Mol. Biol. Cell 10.1091/mbc.E04-12-1117

A more recent version of this article appeared on July 1, 2005
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Submitted on December 27, 2004
Revised on April 11, 2005
Accepted on April 26, 2005

Dynamin Forms a Src-Kinase-sensitive Complex with Cbl and Regulates Podosomes and Osteoclast Activity

Angela Bruzzaniti, Lynn Neff, Archana Sanjay, William C. Horne, Pietro De Camilli, and Roland Baron

Departments of Cell Biology and Orthopedics, Yale University School of Medicine, New Haven, CT 06510

Monitoring Editor: Paul Matsudaira

Podosomes are highly dynamic actin-containing adhesion structures found in osteoclasts, macrophages and RSV-transformed fibroblasts. Following integrin engagement, Pyk2 recruits Src and the adaptor protein Cbl, forming a molecular signaling complex which is critical for cell migration, and deletion of any molecule in this complex disrupts podosome ring formation and/or decreases osteoclast migration. Dynamin, a GTPase essential for endocytosis, is also involved in actin cytoskeleton remodeling and is localized to podosomes where it has a role in actin turnover. We found that dynamin colocalizes with Cbl in the actin-rich podosome belt of osteoclasts and that dynamin forms a complex with Cbl in osteoclasts and when overexpressed in 293VnR or SYF cells. The association of dynamin with Cbl in osteoclasts was decreased by Src tyrosine kinase activity and we found that destabilization of the dynamin-Cbl complex involves the recruitment of Src through the proline-rich domain of Cbl. Overexpression of dynamin increased osteoclast bone resorbing activity and migration while overexpression of dynK44A decreased osteoclast resorption and migration. These studies suggest that dynamin, Cbl and Src coordinately participate in signaling complexes which are important in the assembly and remodeling of the actin cytoskeleton, leading to changes in osteoclast adhesion, migration and resorption.

Address correspondence to: Angela Bruzzaniti (angela.bruzzaniti{at}yale.edu)




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