Peroxisomes are nearly ubiquitous organelles with a variety of metabolic functions including the degradation of fatty acids. I study peroxisome biogenesis in the yeast Saccharomyces cerevisiae. In particular, I am interested in proteins and membranes required for the formation of peroxisomes in the absence of pre-existing peroxisomes. To identify these molecules I will perform genetic screens as well as biochemical reconstitution experiments.
Peroxisomes are ubiquitous eukaryotic organelles which serve in beta-oxidation of fatty acids, hydrogen peroxide-based respiration and oxidative stress defense. In my study, an in vitro vesicle formation assay will be set up to identify ER-derived pre-peroxisomal vesicles. Furthermore the molecular mechanism will be studied by fractionating any cytosolic proteins (e.g. Pex19) required for budding of pre-peroxisomal vesicles.
Mammalian cells secrete proteins mainly through the conventional ER–Golgi secretory pathway. However, some cytoplasmic proteins are released in an unconventional manner independent of ER and Golgi. Autophagy, a cellular process characterized by de novo formation of double membrane structures for intracellular material degradation, contributes to one aspect of unconventional secretion, such as the secretion of IL-1beta. However, the molecular mechanism of autophagy-mediated protein secretion is unclear. Using IL-1beta as a marker, I plan to establish a cell-free system to uncover the mechanism of autophagy-related unconventional secretion.
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