Cited by 153Mitochondrial Function and PathologyAutophagy in Disease and TherapyIon Channels and Receptors

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Mitochondrial matrix Ca 2 + as an intrinsic signal regulating mitochondrial motility in axons

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Chang, Karen T., Niescier, Robert F., Min, Kyung-Tai·2011·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1106862108PMC PMC3174631

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Abstract

The proper distribution of mitochondria is particularly vital for neurons because of their polarized structure and high energy demand. Mitochondria in axons constantly move in response to physiological needs, but signals that regulate mitochondrial movement are not well understood. Aside from producing ATP, Ca 2+ buffering is another main function of mitochondria. Activities of many enzymes in mitochondria are also Ca 2+ -dependent, suggesting that intramitochondrial Ca 2+ concentration is important for mitochondrial functions. Here, we report that mitochondrial motility in axons is actively regulated by mitochondrial matrix Ca 2+ . Ca 2+ entry through the mitochondrial Ca 2+ uniporter modulates mitochondrial transport, and mitochondrial Ca 2+ content correlates inversely with the speed of mitochondrial movement. Furthermore, the miro1 protein plays a role in Ca 2+ uptake into the mitochondria, which subsequently affects mitochondrial movement.

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A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
Stefani, D. D., Raffaello, A., Teardo, E., Szabó, I., & Rizzuto, R. (2011) · Nature · doi:10.1038/nature10230 · Cited by 1,957
Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter
Baughman, J. M., Perocchi, F., Girgis, H. S., Plovanich, M., Belcher-Timme, C. A., Sancak, Y., Bao, X. R., Strittmatter, L., Goldberger, O., Bogorad, R. L., et al. (2011) · Nature · doi:10.1038/nature10234 · Cited by 1,953
A high signal-to-noise Ca2+ probe composed of a single green fluorescent protein
Nakai, J., Ohkura, M., & Imoto, K. (2001) · Nature Biotechnology · doi:10.1038/84397 · Cited by 1,619
The mitochondrial calcium uniporter is a highly selective ion channel
Kirichok, Y., Krapivinsky, G., & Clapham, D. E. (2004) · Nature · doi:10.1038/nature02246 · Cited by 1,409
Role of calcium ions in regulation of mammalian intramitochondrial metabolism
McCormack, J. G., Halestrap, A. P., & Denton, R. M. (1990) · Physiological Reviews · doi:10.1152/physrev.1990.70.2.391 · Cited by 1,398
The axonal transport of mitochondria
Saxton, W. M., & Hollenbeck, P. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.053850 · Cited by 1,218
Mitochondria in neuroplasticity and neurological disorders
Mattson, M. P., Gleichmann, M., & Cheng, A. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.010 · Cited by 1,081
MICU1 encodes a mitochondrial EF hand protein required for Ca2+ uptake
Perocchi, F., Gohil, V. M., Girgis, H. S., Bao, X. R., McCombs, J. E., Palmer, A. E., & Mootha, V. K. (2010) · Nature · doi:10.1038/nature09358 · Cited by 888
The Mechanism of Ca2+-Dependent Regulation of Kinesin-Mediated Mitochondrial Motility
Wang, X., & Schwarz, T. L. (2009) · Cell · doi:10.1016/j.cell.2008.11.046 · Cited by 871
Regulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming
Jouaville, L. S., Pinton, P., Bastianutto, C., Rutter, G. A., & Rizzuto, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13807 · Cited by 831

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Authors: Chang, K. T., Niescier, R. F., & Min, K.-T.
Affiliations: University of Southern California (US)
Indiana University Bloomington (US)
ORCID: Chang, Karen T.
Niescier, Robert F.
Min, Kyung-Tai
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2011-08-29
Volume: 108
Issue: 37
Pages: 15456-15461
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.1106862108
PMC: PMC3174631
OpenAlex: W1998654006
Cited by: 153
References: 33
Citations by year: 2026: 9 · 2025: 15 · 2024: 13 · 2023: 11 · 2022: 13 · 2021: 14 · 2020: 10 · 2019: 12 · 2018: 8 · 2017: 7 · 2016: 10 · 2015: 5 · 2014: 12 · 2013: 6 · 2012: 8
FWCI: 3.37
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Scholarworks@UNIST (Ulsan National Institute of Science and Technology) (submittedVersion)
Funders: National Institute of Neurological Disorders and Stroke (K99NS052524, NS052524, R00NS052524)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords: mitochondrial motility, axons, mitochondrial matrix calcium, mitochondrial calcium uniporter, calcium uptake, Miro1, mitochondrial transport, calcium buffering, neuronal energy metabolism, calcium-dependent enzyme activity
MeSH terms: Animals, Axons, Calcium, Humans, Mitochondria, Movement, Mutation, Calcium Channels, Calcium Signaling, EF Hand Motifs, Mitochondrial Proteins, Mice

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Mitochondrial matrix Ca 2 + as an intrinsic signal regulating mitochondrial motility in axons

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