Ovarian Cancer Lipid raft proteomics and role of OPCML

ipid rafts are dynamic membrane micro-domains that orchestrate molecular interactions and are implicated in cancer development. To understand potential role of tumor suppressor OPCML on the altered dynamics of lipid raft residing proteins, we performed quantitative (SILAC) proteomics experiment. We recently found that OPCML negatively regulates a subset of receptor tyrosine kinases (RTKs) by altering their recycling and ubiquitin-mediated degradation via sequestration to lipid rafts; however, the molecular mechanism linking OPCML tumor suppressor expression to altered RTK trafficking remains unclear. Here we performed a quantitative lipid raft proteomics study to dissect raft-mediated mechanism of OPCML-regulated tumor suppression. We also examined raft-associated mechanism of OPCML P95R, a common mutation resulting in substitution of proline to arginine at position 95, mediated regulation of adhesion potential of tumors.