We utilize both budding yeast and mammalian cellular systems to study receptor trafficking, and more generally membrane reshaping. As a post-doc in the laboratory of Scott Emr, Ph.D., at Cornell University, Mike conducted a global screen in budding yeast to uncover novel proteins involved in the endolysosomal trafficking of receptors.
We used Mup1-pHluorin, a plasma membrane methionine permease, as a well-characterized model receptor that displays inducible endolysosomal sorting upon addition of exogenous methionine.
Using Mup1-pHluorin, we uncovered genes whose deletion causes the mis-sorting of Mup1-pHluorin to the acidic interior of the yeast lysosome/vacuole.
Future studies will dissect the mechanistic roles of these genes in endolysosomal trafficking, and their roles in mammalian endolysosomal trafficking.