Evidence map›Paper›PMID 24514027›Full record

ArticleThe EMBO journal2014

Structural and mechanistic insights into MICU1 regulation of mitochondrial calcium uptake.

Lele Wang, Xue Yang, Siwei Li, Zheng Wang, Yu Liu, Jianrong Feng, Yushan Zhu, Yuequan Shen

Abstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

79 citing papers in PubMed.

  1. Article
  2. Mitochondrial CaJournal of cellular physiology · 2025
    Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. The mitochondrial CaEMBO reports · 2021
    Article
  17. Article
  18. mtROS InducedFrontiers in immunology · 2021
    Article
  19. Review
  20. Regulation of CaCurrent opinion in physiology · 2020
    Article

19 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Lele WangState Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.
Xue Yang
Siwei Li
Zheng Wang
Yu Liu
Jianrong Feng
Yushan Zhu
Yuequan Shen

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial calcium uptake is a critical event in various cellular activities. Two recently identified proteins, the mitochondrial Ca(2+) uniporter (MCU), which is the pore-forming subunit of a Ca(2+) channel, and mitochondrial calcium uptake 1 (MICU1), which is the regulator of MCU, are essential in this event. However, the molecular mechanism by which MICU1 regulates MCU remains elusive. In this study, we report the crystal structures of Ca(2+)-free and Ca(2+)-bound human MICU1. Our studies reveal that Ca(2+)-free MICU1 forms a hexamer that binds and inhibits MCU. Upon Ca(2+) binding, MICU1 undergoes large conformational changes, resulting in the formation of multiple oligomers to activate MCU. Furthermore, we demonstrate that the affinity of MICU1 for Ca(2+) is approximately 15-20 μM. Collectively, our results provide valuable details to decipher the molecular mechanism of MICU1 regulation of mitochondrial calcium uptake.

Indexed as

Models, MolecularProtein ConformationBlotting, WesternCalciumCalcium-Binding ProteinsCalcium ChannelsCalorimetryCation Transport ProteinsCrystallizationEscherichia coliHEK293 CellsHeLa CellsHumansImmunoprecipitationMitochondriaMitochondrial Membrane Transport ProteinsCalciumCalcium-Binding ProteinsCalcium ChannelsCation Transport ProteinsMICU1 protein, humanmitochondrial calcium uniporterMitochondrial Membrane Transport Proteins

Identifiers

PMID24514027
PMCPMC3989653

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.