Ah Young, Andrew P.
Andrew is in the Department of Biological Chemistry. He joined the training program in 2013. His research mentor is Dr. Pascal Egea. He received a B.S. degree in 2009 from U. New Mexico, Albuquerque.
Mentor: Dr. Pascal Egea
One of the hallmarks of eukaryotic cells is the presence of membranebound organelles and their exquisite compartmentalization. Organelles create optimized environments that are required for the catalysis of specialized biochemical reactions. However, in order for the cell to function as one unit, organelles must communicate to allow the exchange of metabolites and other cellular cues. The physical association, or tethering, between organelles is an essential and efficient route for intracellular communication, and has been extensively studied at the cellular level. These zones of physical contact are mediated by membrane protein complexes and have been observed at the interface of the nucleus-vacuole, ER-plasma membrane, and ER-mitochondria, suggesting a global paradigm for protein-mediated, inter-organelle communication. The formation of these contact sites is physiologically significant; association between the ER and mitochondria is required for the transport of calcium, maintenance of mitochondrial morphology, and synthesis and exchange of phospholipids. Genetic evidence argues that perturbations affecting the physical links between the ER and mitochondria are associated with neurodegenerative disorders, such as Alzheimer and Charcot Marie Tooth Type IIA and cancer. Despite the biological and medical relevance of inter-organelle membrane contact sites, we lack detailed structural information about any of the membrane-tethering complexes identified to date.
Using a combination of structural and biochemical tools, my research seeks to understand how organelles communicate by investigating a mechanism of membrane-tethering in a novel model system: the ER-mitochondria encounter structure (ERMES), a membrane-associated ER-mitochondria tethering complex. Specifically, my work seeks to characterize the structure and function of the synaptotagmin-like, mitochondrial and lipid-binding protein (SMP) domain – a signature feature of ERMES constituents – also observed in other tethering complexes in eukaryotes.
