My lab is interested in understanding a fundamental pathway known as endoplasmic reticulum-specific autophagy, or ER-phagy. The ER is one of the largest organelles that performs a myriad of important functions and is tightly controlled by sophisticated quality control pathways, including the ER-associated degradation (ERAD) and unfolded protein response pathway. In recent years, it has been shown that damaged or superfluous ER can also be specifically degraded via ER-phagy. Clinical mutations of ER-phagy regulators are associated with pathologies such as neurodevelopment defects, pancreatic stress, and cancer metastasis.
The overarching interests of my lab are:
- To identify and characterize novel factors that regulate ERphagy
- To explore the physiological and pathological implications of ERphagy
My lab will use state-of-the-art CRISPR-based gene editing and genome-wide screening technology, fluorescence-activated cell sorting (FACS), mass spectrometry, fluorescence microscopy, and various biochemical assays to interrogate ERphagy in different cell types.
One of the immediate focuses of my group will stem from my previous work. I previously demonstrated that UFMylation, a form of Ubiquitin-like modification, serves as an ER quality control pathway that triggers ERphagy upon accumulation of ER stress. My lab will further expand on this discovery and explore various aspects of UFMylation, ranging from the upstream sensing pathways, cross-talk with other ER stress pathways, and the physiological importance of UFMylation-mediated ERphagy.