The DOI matches its Crossref record; 186 of the 186 references it cites were found in a registry or an index.
Mitochondrial cholesterol: mechanisms of import and effects on mitochondrial function
Abstract
Mitochondria require cholesterol for biogenesis and membrane maintenance, and for the synthesis of steroids, oxysterols and hepatic bile acids. Multiple pathways mediate the transport of cholesterol from different subcellular pools to mitochondria. In steroidogenic cells, the steroidogenic acute regulatory protein (StAR) interacts with a mitochondrial protein complex to mediate cholesterol delivery to the inner mitochondrial membrane for conversion to pregnenolone. In non-steroidogenic cells, several members of a protein family defined by the presence of a StAR-related lipid transfer (START) domain play key roles in the delivery of cholesterol to mitochondrial membranes. Subdomains of the endoplasmic reticulum (ER), termed mitochondria-associated ER membranes (MAM), form membrane contact sites with mitochondria and may contribute to the transport of ER cholesterol to mitochondria, either independently or in conjunction with lipid-transfer proteins. Model systems of mitochondria enriched with cholesterol in vitro and mitochondria isolated from cells with (patho)physiological mitochondrial cholesterol accumulation clearly demonstrate that mitochondrial cholesterol levels affect mitochondrial function. Increased mitochondrial cholesterol levels have been observed in several diseases, including cancer, ischemia, steatohepatitis and neurodegenerative diseases, and influence disease pathology. Hence, a deeper understanding of the mechanisms maintaining mitochondrial cholesterol homeostasis may reveal additional targets for therapeutic intervention. Here we give a brief overview of mitochondrial cholesterol import in steroidogenic cells, and then focus on cholesterol trafficking pathways that deliver cholesterol to mitochondrial membranes in non-steroidogenic cells. We also briefly discuss the consequences of increased mitochondrial cholesterol levels on mitochondrial function and their potential role in disease pathology.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The ER is well known in steroidogenic research as the site of action of numerous steroidogenic CYP and HSD/KSR enzymes (3), but recently, the ER has attracted recent interest in mitochondrial cholesterol metabolism as a possible source of cholesterol (147).”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [147]
Citations
Cites
Regulation of cancer cell metabolism
Cairns, R. A., Harris, I. S., & Mak, T. W. (2011) · Nature Reviews Cancer · doi:10.1038/nrc2981 · Cited by 4,744
Otto Warburg's contributions to current concepts of cancer metabolism
Koppenol, W. H., Bounds, P. L., & Dang, C. V. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3038 · Cited by 3,427
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257
Cellular cholesterol trafficking and compartmentalization
Ikonen, E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2336 · Cited by 1,506
Links between metabolism and cancerPreprint
Dang, C. V. (2012) · Genes & Development · doi:10.1101/gad.189365.112 · Cited by 1,021
Mitochondrial Glutathione, a Key Survival Antioxidant
Marí, M., Morales, A., Colell, A., García‐Ruiz, C., & Fernández-Checa, J. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2695 · Cited by 1,006
Horvath, S. E., & Daum, G. (2013) · Progress in Lipid Research · doi:10.1016/j.plipres.2013.07.002 · Cited by 943
MAM: more than just a housekeeper
Hayashi, T., Rizzuto, R., Hajnoczky, G., & Su, T.-P. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.12.002 · Cited by 787
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–128 of 128
Yang, W., Liu, S., Shang, D., Liu, P., Shi, H., Zhang, H., & Chao Hui, Z. H. O. U. (2026) · BMC Molecular and Cell Biology · doi:10.1186/s12860-026-00566-y · Cited by 3
Särndahl, E., Bergman, E., Kotlyar, O., Karlsson, P., Zetzsche, J., Wu, R., Engwall, M., Hyötyläinen, T., & Alijagić, A. (2026) · Environment International · doi:10.1016/j.envint.2026.110370 · Cited by 3
Mitochondrial Functionality Is Regulated by Alkylphospholipids in Human Colon Cancer Cells
Torrens‐Mas, M., Collado-Solé, A., Sola‐Leyva, A., Carrasco-Jimenez, M. P., Oliver, J., Pons, D. G., Roca, P., & Sastre‐Serra, J. (2023) · Biology · doi:10.3390/biology12121457 · Cited by 3
Kennedy, B. E., Charman, M., & Karten, B. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6875-6_12 · Cited by 4
Self-citationSLC25A46 is in contact with lysosomes and plays a role in mitochondrial cholesterol homeostasisPreprint
Schuettpelz, J., Watt, K., Antonická, H., Janer, A., Larsson, O. S., & Shoubridge, E. A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.01.587618 · Cited by 3
Aly, A. S., Rozeboom, K. J., & Parrish, J. J. (2025) · Animals · doi:10.3390/ani15142038 · Cited by 2
Yang, N. V., Rogers, S. W., Guerra, R. M., Chao, J. Y., Pagliarini, D. J., Theusch, E., & Krauss, R. M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262210977 · Cited by 2
Aspectos generales del transporte de colesterol en la esteroidogénesis de la placenta humana
Olvera-Sánchez, S., Esparza-Perusquía, M., Flores-Herrera, Ó., Urban-Sosa, V. A., & Martı́nez, F. (2019) · TIP Revista Especializada en Ciencias Químico-Biológicas · doi:10.22201/fesz.23958723e.2019.0.180 · Cited by 2
Cholesterol metabolism in prostate cancer
Koltai, T., Reshkin, S. J., Baltazar, F., & Fliegel, L. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-90528-2.00007-2 · Cited by 2
Kakouri, A. C., Votsi, C., Oulas, A., Nicolaou, P., Aureli, M., Lunghi, G., Samarani, M., Compagnoni, G. M., Salani, S., Fonzo, A. D., et al. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00754-1 · Cited by 2
Li, J., Hao, X., Xiao, T. H., & Zhu, B. T. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.110790 · Cited by 2
Mitochondrial toxicity of aflatoxin B1
Rotimi, O. A., Adelani, I. B., Campos, O. C. D., Olawole, T. D., & Rotimi, S. O. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-88462-4.00023-7 · Cited by 1
Cardiomyocyte-specific PCSK9 deficiency compromises mitochondrial bioenergetics and heart function
Laudette, M. (2022) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2022.08.348 · Cited by 1
Impact of Cholesterol on Cardiac Mitochondrial Function
Lopaschuk, G. D. (2025) · Circulation Research · doi:10.1161/circresaha.125.326464 · Cited by 1
Bisht, K., Sahu, R., Vasudevan, S., Jit, S., Bhor, N., Kumar, J., Madan, M., Shankaran, D., Bhalla, S., Chandra, N. R., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.18.665474 · Cited by 1
Characterization of oxysterols produced in macrophages and mechanisms of regulation
Chen, Y. (2016) · theses.fr (ABES) · doi:10.70675/379acbf2z8e6cz41dbza8eaza1ac615d59cd · Cited by 1
Митохондриальные нарушения при болезни Альцгеймера
Sukhorukov, V. S., Mudzhiri, N. M., Voronkova, A. S., Baranich, T. I., Glinkina, V. V., & Illarioshkin, S. N. (2021) · Biochemistry (Moscow) · doi:10.31857/s0320972521060051
Single-cell analyses reveal tissue-specific contextualization of HIF-1 activityPreprint
Kong, J. N., Ghosh, D. D., Ma, D., Kesisova, I. A., Dwivedi, V. K., Savvidis, A., Sando, S. R., Guerra, L., & Horvitz, H. R. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.02.601765
Villanueva-Rodríguez, R., Valdez, A. V., Martinez, M. C., Corrales, L. L. P., Aguilar, R. D. L. S., & Oliva, L. D. S. (2024) · Case Reports in Endocrinology · doi:10.1155/2024/5399577
Ahmed, S. H. H., Mohamed, H. A., Attia, G. M., & El-Bassouny, D. R. (2025) · Ultrastructural Pathology · doi:10.1080/01913123.2025.2584119
Krüger, A. F., Schmitz, W., Lamer, S., Triebig, A. S., Maier, T., Fuß, C. T., Angeli, J. P. F., Schlösser, A., Stigloher, C., Faßnacht, M., et al. (2025) · Journal of the Endocrine Society · doi:10.1210/jendso/bvaf198 · Cited by 1
Roland, N. J., Zigmond, J. W., Manganaro, J. E., Estrella, L. D., & Stauch, K. L. (2026) · Neurochemistry International · doi:10.1016/j.neuint.2026.106125 · Cited by 1
Li, W., Zhang, H. D., Guo, Z., Wang, Y., Yang, H., & Wang, Z. (2026) · Italian Journal of Animal Science · doi:10.1080/1828051x.2026.2632025
Kiriyama, Y., Nakatsuma, A., Tokumaru, H., Sadamoto, H., & Nochi, H. (2026) · Metabolites · doi:10.3390/metabo16030189
Étude de la fonction mitochondriale des macrophages au cours de l'athérosclérose
Becker, P. (2022) · theses.fr (ABES) · doi:10.70675/0bff8b92z95b0z44daz8f52z9e5d3eec2879
Dreßen, M., Northoff, B. H., Lahm, H., Gottmann, I., Richter, S., Bharne, D., Wirth, F., Goppel, G., Seeler, S., Dzilic, E., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-11267708/v1
Mitochondrial toxicity of aflatoxin B1
Rotimi, O. A., Adelani, I. B., Campos, O. C. D., Olawole, T. D., & Rotimi, S. O. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-45078-5.00020-8
Metadata
- Authors
- Martin, L. A., Kennedy, B. E., & Karten, B.
- Affiliations
- Dalhousie University (CA)
- Corresponding author
- Karten, Barbara
- ORCID
- Karten, Barbara
- Venue
- Journal of Bioenergetics and Biomembranes
- Published
- 2014-11-26
- Volume
- 48
- Issue
- 2
- Pages
- 137-151
- ISSN
- 0145-479X (ISSN-L)
- 1573-6881
- OpenAlex
- W1993948951
- Cited by
- 128
- References
- 186
- Citations by year
- 2026: 8 · 2025: 16 · 2024: 10 · 2023: 13 · 2022: 21 · 2021: 20 · 2020: 9 · 2019: 10 · 2018: 5 · 2017: 8 · 2016: 4 · 2015: 3 · 2014: 1
- FWCI
- 1.01
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Journal of Bioenergetics and Biomembranes (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- mitochondrial cholesterol, steroidogenic acute regulatory protein, mitochondria-associated ER membranes, lipid transfer proteins, mitochondrial function, oxysterols, bile acids, mitochondrial membrane
- MeSH terms
- Steroidogenic Acute Regulatory Protein, Animals, Biological Transport, Active, Cholesterol, Endoplasmic Reticulum, Humans, Mitochondria, Phosphoproteins, Mitochondrial Membranes
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
