For two decades, my laboratory has been developing tools to help understanding the cell biology of signaling networks. Our techniques permit the visualization as well as the non-invasive manipulation of intact cells. Since several years, one focus of our work is to understand how growth factor signaling, for instance by epidermal growth factor(EGF), is partially mediated and ultimately terminated by receptor internalization. In 2014, we published the finding that elevated levels of the signaling lipid phosphatidylinositol 3,4,5-trisphosphate (PIP3) comprised a sufficient signal to induce EGF receptor (EGFR) internalization. Interestingly, this internalization in the absence of tyrosine phosphorylation and ubiquitination leads to full recycling of the receptor. We speculate that such a scenario is relevant in cells that require ongoing growth factor signaling such as the growth cone of an axon but also late stage cancer cells where mutations in a PIP3-modulating enzyme such as PTEN lead to increased signaling and proliferation.
Our move to Portland brings us close to a vibrant scientific community interested in cancer research. Therefore, we would like to continue our studies on EGFR internalization and find out what lipids and proteins are involved in mediating the PIP3 signal to the endocytic machinery and what molecular epitope of the EGFR is recognized to make EGFR a cargo.Read more
- Ph.D., Chemistry, Bremen University, Germany 1989
- 1990-93 Postdoctoral, Pharmacology, University of California San Diego