The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Structure and mechanism of the mitochondrial Ca2+ uniporter holocomplex
Open accessAbstract
Mitochondria take up Ca2+ through the mitochondrial calcium uniporter complex to regulate energy production, cytosolic Ca2+ signalling and cell death1,2. In mammals, the uniporter complex (uniplex) contains four core components: the pore-forming MCU protein, the gatekeepers MICU1 and MICU2, and an auxiliary subunit, EMRE, essential for Ca2+ transport3–8. To prevent detrimental Ca2+ overload, the activity of MCU must be tightly regulated by MICUs, which sense changes in cytosolic Ca2+ concentrations to switch MCU on and off9,10. Here we report cryo-electron microscopic structures of the human mitochondrial calcium uniporter holocomplex in inhibited and Ca2+-activated states. These structures define the architecture of this multicomponent Ca2+-uptake machinery and reveal the gating mechanism by which MICUs control uniporter activity. Our work provides a framework for understanding regulated Ca2+ uptake in mitochondria, and could suggest ways of modulating uniporter activity to treat diseases related to mitochondrial Ca2+ overload. Cryo-electron microscopy reveals the structures of the mitochondrial calcium uniporter holocomplex in low- and high-calcium conditions, showing the gating mechanism that underlies uniporter activation in response to intracellular calcium signals.
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Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
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Mitochondria as sensors and regulators of calcium signalling
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Baev, A. Y., Vinokurov, A. Y., Novikova, I. N., Dremin, V. V., Potapova, E. V., & Abramov, A. Y. (2022) · Cells · doi:10.3390/cells11040706 · Cited by 162
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Metadata
- Authors
- Fan, M., Zhang, J., Tsai, C.-W., Orlando, B. J., Rodriguez, M., Xu, Y., Liao, M., Tsai, M.-F., & Feng, L.
- Venue
- Nature
- Published
- 2020-05-20
- Volume
- 582
- Issue
- 7810
- Pages
- 129-133
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W3026314418
- Cited by
- 305
- References
- 5
- FWCI
- 10.65
- Type
- journal article
- Language
- en
- Open access
- green
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