David Gross
Biography
We primarily study the epidermal growth factor receptor (EGFR), a member of the tyrosine kinase receptor family. This 170 kDa receptor has an extracellular ligand binding domain, a single transmembrane spanning region, and an intracellular domain containing the tyrosine kinase and a regulatory subdomain. Within the regulatory region are five tyrosines that, when transphosphorylated by other EGFR, become SH2 docking sites for various signaling molecules. The EGFR is also known to be an actin binding molecule. We employ quantitative fluorescence imaging, electrophysiology, recombinant DNA techniques, and biochemistry in our studies. We are working on effects of point mutations within the actin-binding domain of the EGFR on cellular endpoints such as control of EGFR ligand affinity, internalization, cell surface mobility and cytoskeletal interactions. We have made a green fluorescent protein-EGFR fusion protein that is useful for following EGFR processing (see figure). Other studies include examination of the role of EGFR on oocyte in vitro maturation and synthesis of a polyelectrolyte-EGF that may be useful in disrupting the endocytic pathway. My research has transitioned from laboratory and theoretical study of receptor-mediated second-messenger signaling in individual cells to STEM classroom pedagogies to improve student learning outcomes. Incorporation of active learning techniques in combination with blended course materials and collaborative learning pedagogies are the tools that I use in my classes to enhance the student experience and student learning outcomes for all students, particularly for students who have struggled in other courses. I study the mechanisms by which improvement of learning outcomes occur and I experiment with pedagogies and learning technologies to refine my instruction.EDUCAUSE Presentations
Membership with EDUCAUSE
| Status: | Yes, current member |