Regulation of the formation of osteoclastic actin rings by proline-rich tyrosine kinase 2 interacting with gelsolin

• DOI: 10.1083/jcb.200207036
• Publication Date: 2003-02-18T19:45:08Z
• Authors: Qiang Wang; Yi Xie; Quan-Sheng Du; Xiao-Jun Wu; Xu Feng; Lin Mei; Jay M. McDonald; Wen-Cheng Xiong
• Keywords: Gelsolin; Actin remodeling; Actin-binding protein; PTK2

Osteoclast activation is important for bone remodeling and altered in multiple disorders. This process requires cell adhesion extensive actin cytoskeletal reorganization. Proline-rich tyrosine kinase 2 (PYK2), a major adhesion–activated osteoclasts, plays an role regulating this event. The mechanisms by which PYK2 regulates organization osteoclastic remain largely unknown. In paper, we provide evidence that directly interacts with gelsolin, binding, severing, capping protein essential organization. interaction mediated via the focal adhesion–targeting domain of LD motif gelsolin's COOH terminus. phosphorylates gelsolin at residues bioactivity, including decreasing binding to monomer increasing phosphatidylinositol lipids. addition, increases polymerization fibroblastic periphery. Finally, where required formation rings. Together, our results suggest regulator revealing novel PYK2–gelsolin pathway cells, osteoclasts.