이창욱 연구실

Our long-term goal is to better understand the molecular and cellular mechanisms that underlie the principles for interorganelle communication in the organelle/membrane contact sites. We investigate how protein machinery facilitates organelle specific membrane contacts by determining the atomic resolution structures of protein complexes. Membrane contact sites (MCSs) play an essential role in subcellular communication by exchanging cellular materials and information. Among the various endoplasmic reticulum (ER)-mediated MCSs reported to date, the ER-mitochondria contact site has been the most extensively studied, and an involvement in ion homeostasis, mitochondrial dynamics such as membrane fission and fusion, and cooperative lipid synthesis has been reported. Most importantly, lipid trafficking occurring at the ER-mitochondria MCS is essential for the biogenesis of the mitochondrial membrane, since mitochondria are not connected with the vesicular transport machinery, and essential lipids required for the composition of mitochondrial membrane must therefore be supplied directly from the ER. Our group determined crystal structures of the Mmm1 SMP domain and the Mdm12–Mmm1 binary complex, which are key components of the ER-Mitochondria Encounter Structure (ERMES) complex that play a pivotal role in establishing direct membrane contact sites between the ER and mitochondria. Our laboratory focuses on the structural, biochemical and functional basis of proteins involved in membrane trafficking, mitochondria dynamics and autophagy in eukaryotic cells. In addition, we are interested in elucidating the structure and function of newly discovered cancer-related proteins. We use X-ray crystallography to determine protein structure and we use biochemical analysis to elucidate thei