My research investigates the molecular mechanisms of membrane trafficking from endosomes to lysosomes, which have a major role in protein degradation. Transmembrane proteins ubiquitinated on their cytoplasmic domains are sorted into vesicles that bud into the lumen of endosomes, resulting in their degradation upon fusion of endosomes with lysosomes. Molecular recognition of ubiquitinated transmembrane proteins requires an elaborate machinery known as the endosomal sorting complexes required for transport (ESCRTs). Defects in the ESCRT machinery make profound contributions to human disease. My research on ESCRTs uses the model system Saccharomyces cerevisiae and a combination of genetics, cell biology, biochemistry, and electron tomographic modeling of membrane structures.
membrane trafficking, membrane scission, membrane tethering, membrane fusion, protein ubiquitination, protein deubiquitination