Our lab focuses on the function of the proteins that control plasma membrane function. We have on-going projects investigating ARH/LDLR endocytosis and caveolae signal transduction.
We study the mechanisms by which the protein ARH supports LDLR-dependent LDL uptake, but is dispensable for LDLR-dependent VLDL uptake.
Our research has shown how the LDLR responds to low pH and low calcium concentrations to release lipoprotein in endocytic vesicles.
By modifying amino acid residues of the helical protein ankyrin (ANK), we can alter its shape. We are now developing engineered ANK-repeat protein springs for making nanodevices.
Cavin-3 is a tumor suppressor protein whose loss leads to cachexia (wasting), a frequent cause of death in cancer.