The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Endophilin B1 is required for the maintenance of mitochondrial morphology
Open accessAbstract
We report that a fatty acyl transferase, endophilin B1, is required for maintenance of mitochondrial morphology. Down-regulation of this protein or overexpression of endophilin B1 lacking the NH2-terminal lipid-modifying domain causes striking alterations of the mitochondrial distribution and morphology. Dissociation of the outer mitochondrial membrane compartment from that of the matrix, and formation of vesicles and tubules of outer mitochondrial membrane, was also observed in both endophilin B1 knockdown cells and after overexpression of the truncated protein, indicating that endophilin B1 is required for the regulation of the outer mitochondrial membrane dynamics. We also show that endophilin B1 translocates to the mitochondria during the synchronous remodeling of the mitochondrial network that has been described to occur during apoptosis. Double knockdown of endophilin B1 and Drp1 leads to a mitochondrial phenotype identical to that of the Drp1 single knockdown, a result consistent with Drp1 acting upstream of endophilin B1 in the maintenance of morphological dynamics of mitochondria.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Olichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., & Lenaers, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200677200 · Cited by 1,168
Karbowski, M., Lee, Y.-J., Gaume, B., Jeong, S.-Y., Frank, S., Nechushtan, A., Santel, A., Fuller, M., Smith, C. L., & Youle, R. J. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200209124 · Cited by 846
Self-citationKarbowski, M., Arnoult, D., Chen, H., Chan, D. C., Smith, C. L., & Youle, R. J. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200309082 · Cited by 433
Self-citationDynamin-like protein 1 is involved in peroxisomal fission
Koch, A., Thiemann, M., Grabenbauer, M., Yoon, Y., McNiven, M. A., & Schrader, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211761200 · Cited by 374
Mammalian Dynamin-like Protein DLP1 Tubulates Membranes
Yoon, Y., Pitts, K. R., & McNiven, M. A. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.9.2894 · Cited by 285
Habermann, B. (2004) · The EMBO Reports · doi:10.1038/sj.embor.7400105 · Cited by 281
Cited by
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270
Self-citationMitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission.
Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., & Mihara, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607279200 · Cited by 1,226
Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007152 · Cited by 1,110
Self-citationMitochondria 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
Mitochondrial Fusion and Fission in Mammals
Chan, D. C. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104638 · Cited by 972
Mitochondrial Dynamics in Mammalian Health and Disease
Liesa, M., Palacín, M., & Zorzano, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00030.2008 · Cited by 953
A new pathway for mitochondrial quality control: Mitochondrial-derived vesicles
Sugiura, A., McLelland, G., Fon, E. A., & McBride, H. M. (2014) · The EMBO Journal · doi:10.15252/embj.201488104 · Cited by 862
The Machines that Divide and Fuse Mitochondria
Hoppins, S., Lackner, L., & Nunnari, J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.071905.090048 · Cited by 790
The Interplay Between Mitochondrial Dynamics and Mitophagy
Twig, G., & Shirihai, O. S. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3779 · Cited by 778
MiD49 and MiD51, new components of the mitochondrial fission machinery
Palmer, C. S., Osellame, L. D., Laine, D., Koutsopoulos, O. S., Frazier, A. E., & Ryan, M. T. (2011) · The EMBO Reports · doi:10.1038/embor.2011.54 · Cited by 649
Mitochondrial outer membrane permeabilization during apoptosis: the innocent bystander scenario
Chipuk, J. E., Bouchier-Hayes, L., & Green, D. R. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401963 · Cited by 631
Role of Bax and Bak in mitochondrial morphogenesis
Karbowski, M., Norris, K. L., Cleland, M. M., Jeong, S.-Y., & Youle, R. J. (2006) · Nature · doi:10.1038/nature05111 · Cited by 625
Self-citationThe BAR Domain Superfamily: Membrane-Molding Macromolecules
Frost, A., Unger, V. M., & De Camilli, P. (2009) · Cell · doi:10.1016/j.cell.2009.04.010 · Cited by 574
New insights into the role of mitochondria in aging: mitochondrial dynamics and more
Seo, A. Y., Joseph, A.-M., Dutta, D., Hwang, J. C. Y., Aris, J. P., & Leeuwenburgh, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.070490 · Cited by 522
ITOH, T., & DECAMILLI, P. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.06.015 · Cited by 361
The constriction and scission machineries involved in mitochondrial fission
Kraus, F., & Ryan, M. T. (2017) · Journal of Cell Science · doi:10.1242/jcs.199562 · Cited by 244
Sabogal-Guáqueta, A. M., Hobbie, F., Keerthi, A., Oun, A., Kortholt, A., Boddeke, E., & Dolga, A. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109295 · Cited by 154
Mitochondrial fusion is essential for steroid biosynthesis
Duarte, A., Poderoso, C., Cooke, M., Soria, G., Cornejo Maciel, F., Gottifredi, V., & Podestá, E. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045829 · Cited by 149
WAVE1 controls neuronal activity-induced mitochondrial distribution in dendritic spines
Sung, J. Y., Engmann, O., Teylan, M. A., Nairn, A. C., Greengard, P., & Kim, Y. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712180105 · Cited by 117
BAR the door: Cancer suppression by amphiphysin-like genes
Prendergast, G. C., Muller, A. J., Ramalingam, A., & Chang, M. Y. (2009) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2008.09.001 · Cited by 68
Endophilin-B regulates autophagy during synapse development and neurodegeneration
Hernandez-Diaz, S., Ghimire, S., Sanchez-Mirasierra, I., Montecinos-Oliva, C., Swerts, J., Kuenen, S., Verstreken, P., & Soukup, S.-F. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105595 · Cited by 27
Peripheral membrane protein endophilin B1 probes, perturbs and permeabilizes lipid bilayers
Thorlacius, A., Rulev, M., Sundberg, O., & Sundborger-Lunna, A. (2025) · Communications Biology · doi:10.1038/s42003-025-07610-1 · Cited by 5
Metadata
- Authors
- Karbowski, M., Jeong, S.-Y., & Youle, R. J.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2004-09-27
- Volume
- 166
- Issue
- 7
- Pages
- 1027-1039
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2003705213
- Cited by
- 264
- References
- 6
- FWCI
- 4.37
- Type
- journal article
- Language
- en
- Open access
- green
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
