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.
Coat Protein Complex 2 (COPII) traffics cargo from the ER to the Golgi. I will be studying the role of COPII in trafficking collagen, an example of large cargo. To do this, I will employ the techniques of electron microscopy and molecular biology.
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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