![]() In humans, the uniporter functions as a holocomplex (referred to as uniplex henceforth) and consists of the pore-forming subunit MCU ( Baughman et al., 2011 De Stefani et al., 2011), an essential membrane-spanning subunit EMRE ( Sancak et al., 2013), and the gate-keeping subunits MICU1 ( Perocchi et al., 2010) and MICU2 ( Plovanich et al., 2013). Mitochondrial calcium uptake is mediated by the mitochondrial calcium uniporter, a Ca 2+-selective channel that is localized to the inner mitochondrial membrane ( Gunter and Pfeiffer, 1990 Kirichok et al., 2004). It has long been observed that the vast mitochondrial network takes up large amounts of Ca 2+ from its environment and buffers cytosolic Ca 2+ elevations, thus regulating the spatial and temporal dynamics of intracellular Ca 2+ signaling ( Clapham, 2007 Kamer and Mootha, 2015 Rizzuto et al., 2012). Intracellular Ca 2+ signaling can mediate an array of biological processes ranging from transcriptional and metabolic regulation to cell death ( Berridge et al., 2003). Atomic coordinates for the apo, blocked state. Atomic coordinates for the Ca2+-bound state. human MCU-EMRE-MICU1-MICU2 holocomplex, apo, competing state. human MCU-EMRE-MICU1-MICU2 holocomplex, apo, bridging state. human MCU-EMRE-MICU1-MICU2 holocomplex, apo, blocked state. human MCU-EMRE-MICU1-MICU2 holocomplex, Ca2+-bound state. Atomic coordinates have been deposited in the Protein Data Bank under accession numbers 6XJV for the Ca2+-bound state and 6XJX for the apo, blocked state. ![]() The cryo-EM density maps of the human MCU-EMRE-MICU1-MICU2 holocomplex have been deposited in the Electron Microscopy Data Bank under accession numbers EMD-22215 for the Ca2+-bound state, EMD- 22216 for the apo, blocked state, EMD-22213 for the apo, bridging state and EMD-22214 for the apo, competing state.
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