{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMICU1 is an essential regulatory component of the mitochondrial calcium uniporter (MCU) complex that functions as a Ca²⁺‐sensing “gatekeeper.” Its EF‐hand domains enable it to detect and respond to cytosolic Ca²⁺ elevations, thereby establishing a threshold for mitochondrial Ca²⁺ uptake. In resting conditions, MICU1 prevents excessive accumulation of Ca²⁺ in the mitochondrial matrix that could otherwise trigger overproduction of reactive oxygen species and apoptotic cell death. Conversely, when cytosolic Ca²⁺ rises above a critical level, MICU1 relieves its inhibition on the MCU pore to allow Ca²⁺ entry that is required for metabolic activation and other signaling processes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the molecular level, MICU1 operates via dynamic, Ca²⁺‐dependent structural transitions that are pivotal for proper uniporter gating. Biophysical and structural studies show that upon binding Ca²⁺, MICU1 rearranges its oligomeric state and, in partnership with MICU2, interacts with specific domains of the MCU pore—including a region defined by the DIME motif—to “unlock” the channel. Moreover, MICU1’s interactions with other uniporter partners (such as EMRE) and post‐translational modifications (for example, by Akt or through methylation) further refine its regulatory action. These cooperative and reversible interactions—with demonstrated cooperative, high‐affinity Ca²⁺ binding and structural rearrangements unveiled by cryo‐EM—establish an on–off switch that confers both threshold sensitivity and dynamic range to mitochondrial Ca²⁺ uptake."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its core mechanistic role, alterations in MICU1 expression, splicing, or regulation have profound tissue‐specific and pathological implications. In cancer cells, for instance, MICU1 overexpression promotes metabolic reprogramming toward aerobic glycolysis, while its loss is associated with aberrant Ca²⁺ signaling that contributes to neuromuscular, endocrine, and even neurodegenerative phenotypes. 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