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Dr. Barlowe studies intracellular trafficking and seeks to elucidate basic mechanisms that control protein and lipid transport through the early secretory pathway. His research group investigates this process through a multidisciplinary approach that includes biochemistry, molecular genetics, proteomics and microcopy, primarily in the model organism Saccharomyces cerevisiae. Roughly a quarter of translated proteins enter the secretory pathway at the endoplasmic reticulum (ER) where the coat protein complex II (COPII) selects folded secretory proteins into transport vesicles that bud from the ER for anterograde transport to the Golgi complex. The Barlowe lab has identified and characterized novel membrane receptors that cycle between the ER-Golgi and are needed in concert with the COPII coat to select diverse sets of secretory cargo into ER-derived transport vesicles. Current experimentation is focused on understanding how these membrane receptors recognize specific cargo and howcargo binding is regulated. His laboratory is also interested in defining the mechanisms that target and fuse COPII transport vesicles with the Golgi complex.