| dc.description.abstract | Tumor cells use actin-based structures capable of degrading the extracellular matrix during the process of invasion and metastasis. Recent studies demonstrate that the
adaptor protein Nck-2, an important link between tyrosine phosphorylation and cytoskeletal remodeling, is required for invasion in cancer cells. Using biochemical approaches, we have previously uncovered that the scaffolding protein p62Dok interacts with Nck in transformed (tumor-like) but not normal cells. However, we know very little about this interaction and the role of p62Dok in mechanisms of invasion of cancer cells. We seek to determine if this interaction is important in living cells. We used a combination of molecular genetics, proteomics, and high-resolution optical microscopy to determine the subcellular distribution of p62Dok and to determine if p62Dok is required for tumor cell invasion. We have successfully induced invasive structures in
fibroblasts and have made a fluorescent Dok1 fusion protein. Preliminary data suggest that Dok1 localizes to these invasive structures. Studies are ongoing to prove
conclusively that Dok1 localizes to invasive structures. | en |
