The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
A Role for Fis1 in Both Mitochondrial and Peroxisomal Fission in Mammalian Cells
Open accessAbstract
The mammalian dynamin-like protein DLP1/Drp1 has been shown to mediate both mitochondrial and peroxisomal fission. In this study, we have examined whether hFis1, a mammalian homologue of yeast Fis1, which has been shown to participate in mitochondrial fission by an interaction with DLP1/Drp1, is also involved in peroxisomal growth and division. We show that hFis1 localizes to peroxisomes in addition to mitochondria. Through differential tagging and deletion experiments, we demonstrate that the transmembrane domain and the short C-terminal tail of hFis1 is both necessary and sufficient for its targeting to peroxisomes and mitochondria, whereas the N-terminal region is required for organelle fission. hFis1 promotes peroxisome division upon ectopic expression, whereas silencing of Fis1 by small interfering RNA inhibited fission and caused tubulation of peroxisomes. These findings provide the first evidence for a role of Fis1 in peroxisomal fission and suggest that the fission machinery of mitochondria and peroxisomes shares common components.
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.
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
“DLP-1 has a shared function in peroxisomal and mitochondrial fission, and is recruited to peroxisomes by two mitochondrial-associated fission factors, mitochondrial fission factor (MFF) (Gandre-Babbe and van der Bliek, 2008), and mitochondrial fission 1 (FIS1), following PEX11β-mediated elongation (Koch et al., 2005; Itoyama et al., 2013).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Koch et al., 2005
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
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
The dynamin superfamily: universal membrane tubulation and fission molecules?
Praefcke, G. J. K., & McMahon, H. T. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1313 · Cited by 1,370
Lazarow, P. B., & Fujiki, Y. (1985) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.01.110185.002421 · Cited by 1,114
van den BOSCH, H., Schutgens, R. B. H., Wanders, R. J. A., & Tager, J. M. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.001105 · Cited by 844
Yoon, Y., Krueger, E. W., Oswald, B. J., & McNiven, M. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5409-5420.2003 · Cited by 820
The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast
Bleazard, W., McCaffery, J. M., King, E. J., Bale, S., Mozdy, A. D., Tieu, Q., Nunnari, J. M., & Shaw, J. M. (1999) · Nature Cell Biology · doi:10.1038/13014 · Cited by 795
Mozdy, A. D., McCaffery, J. M., & Shaw, J. M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.2.367 · Cited by 731
C. elegans Dynamin-Related Protein DRP-1 Controls Severing of the Mitochondrial Outer Membrane
Labrousse, A. M., Zappaterra, M. D., Rube, D. A., & van der Bliek, A. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80391-3 · Cited by 670
hFis1, a Novel Component of the Mammalian Mitochondrial Fission Machinery
James, D. I., Parone, P. A., Mattenberger, Y., & Martinou, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303758200 · Cited by 653
Division versus Fusion: Dnm1p and Fzo1p Antagonistically Regulate Mitochondrial Shape
Sesaki, H., & Jensen, R. E. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.4.699 · Cited by 531
Cited by
Sorted by citations
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002
Functions and dysfunctions of mitochondrial dynamics
Detmer, S. A., & Chan, D. C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2275 · Cited by 1,369
Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission
Losón, O. C., Song, Z., Chen, H., & Chan, D. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0721 · Cited by 1,235
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196
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
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
Peroxisomes and oxidative stress
Schrader, M., & Fahimi, H. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.09.006 · Cited by 838
Peroxisomes Are Signaling Platforms for Antiviral Innate Immunity
Dixit, E., Boulant, S., Zhang, Y., Lee, A. S. Y., Odendall, C., Shum, B. O. V., Hacohen, N., Chen, Z. J., Whelan, S. P. J., Fransen, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.04.018 · Cited by 850
Gandre-Babbe, S., & van der Bliek, A. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1287 · Cited by 769
A Lethal Defect of Mitochondrial and Peroxisomal Fission
Waterham, H. R., Koster, J., van Roermund, C. W. T., Mooyer, P. A. W., Wanders, R. J. A., & Leonard, J. V. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa064436 · Cited by 749
Cargo-Selected Transport from the Mitochondria to Peroxisomes Is Mediated by Vesicular Carriers
Neuspiel, M., Schauss, A. C., Braschi, E., Zunino, R., Rippstein, P. U., Rachubinski, R. A., Andrade-Navarro, M. A., & McBride, H. M. (2008) · Current Biology · doi:10.1016/j.cub.2007.12.038 · Cited by 607
mito-QC illuminates mitophagy and mitochondrial architecture in vivo
McWilliams, T. G., Prescott, A. R., Allen, G. F. G., Tamjar, J., Munson, M. J., Thomson, C., Muqit, M. M. K., & Ganley, I. G. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201603039 · Cited by 561
Smith, J. J., & Aitchison, J. D. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3700 · Cited by 470
Use of Dynasore, the Small Molecule Inhibitor of Dynamin, in the Regulation of Endocytosis
Kirchhausen, T. L., Macia, E., & Pelish, H. E. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)38006-3 · Cited by 447
The cell biology of the retinal pigment epithelium
Lakkaraju, A., Umapathy, A., Tan, L. X., Daniele, L., Philp, N. J., Boesze-Battaglia, K., & Williams, D. S. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100846 · Cited by 422
Human disorders of peroxisome metabolism and biogenesis
Waterham, H. R., Ferdinandusse, S., & Wanders, R. J. A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.11.015 · Cited by 384
The Peroxisome-Mitochondria Connection: How and Why?
Fransen, M., Lismont, C., & Walton, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061126 · Cited by 351
“, mitochondrial fission protein (FIS) 1 [45], mitochondrial fission factor (MFF) [46], ganglioside-induced differentiation-associated protein (GDAP) 1 [47], and dynamin 1-like protein (DNM1L) [48,49]) (Figure 1c).”
Dynamin-related protein 1 and mitochondrial fragmentation in neurodegenerative diseases
Reddy, P. H., Reddy, T. P., Mańczak, M., Calkins, M. J., Shirendeb, U. P., & Mao, P. (2010) · Brain Research Reviews · doi:10.1016/j.brainresrev.2010.11.004 · Cited by 372
Palmer, C. S., Elgass, K. D., Parton, R. G., Osellame, L. D., Stojanovski, D., & Ryan, M. T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.479873 · Cited by 301
Vps35 Mediates Vesicle Transport between the Mitochondria and Peroxisomes
Braschi, E., Goyon, V., Zunino, R., Mohanty, A., Xu, L., & McBride, H. M. (2010) · Current Biology · doi:10.1016/j.cub.2010.05.066 · Cited by 319
Structural insights into oligomerization and mitochondrial remodelling of dynamin 1‐like protein
Fröhlich, C., Grabiger, S., Schwefel, D., Faelber, K., Rosenbaum, E., Mears, J. A., Rocks, O., & Daumke, O. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.74 · Cited by 292
The peroxisome: an update on mysteries 2.0
Islinger, M., Völkl, A., Fahimi, H. D., & Schrader, M. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1722-5 · Cited by 296
Genetics and molecular basis of human peroxisome biogenesis disorders
Waterham, H. R., & Ebberink, M. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.04.006 · Cited by 283
The peroxisome: an update on mysteries
Islinger, M., Grille, S., Fahimi, H. D., & Schrader, M. (2012) · Histochemistry and Cell Biology · doi:10.1007/s00418-012-0941-4 · Cited by 283
Human IRGM regulates autophagy and cell-autonomous immunity functions through mitochondria
Singh, S., Ornatowski, W., Vergne, I., Naylor, J., Delgado, M. A., Roberts, E. A., Ponpuak, M., Master, S. S., Pilli, M., White, E., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2119 · Cited by 268
ACBD5 and VAPB mediate membrane associations between peroxisomes and the ER
Costello, J. L., Castro, I. G., Hacker, C., Schrader, T. A., Metz, J., Zeuschner, D., Azadi, A. S., Godinho, L. F., Costina, V., Findeisen, P., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201607055 · Cited by 251
Belgnaoui, S. M., Paz, S., & Hiscott, J. B. (2011) · Current Opinion in Immunology · doi:10.1016/j.coi.2011.08.001 · Cited by 241
Mitochondrial dynamics in the adult cardiomyocytes: which roles for a highly specialized cell?
Piquereau, J., Caffin, F., Novotová, M., Lemaire, C., Veksler, V., Garnier, A., Ventura‐Clapier, R., & Joubert, F. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00102 · Cited by 251
Inhibiting the Mitochondrial Fission Machinery Does Not Prevent Bax/Bak-Dependent Apoptosis
Parone, P. A., James, D. I., Cruz, S. D., Mattenberger, Y., Donzé, O., Barja, F., & Martinou, J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02282-05 · Cited by 231
The physiological functions of human peroxisomes
Wanders, R. J. A., Baes, M., Ribeiro, D., Ferdinandusse, S., & Waterham, H. R. (2023) · Physiological Reviews · doi:10.1152/physrev.00051.2021 · Cited by 228
Mutations in Fis1 disrupt orderly disposal of defective mitochondria
Shen, Q., Yamano, K., Head, B. P., Kawajiri, S., Cheung, J. T. M., Wang, C., Cho, J.-H., Hattori, N., Youle, R. J., & van der Bliek, A. M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-09-0525 · Cited by 209
Dynamin-related proteins Vps1p and Dnm1p control peroxisome abundance inSaccharomyces cerevisiae
Kuravi, K. V., Nagotu, S., Krikken, A. M., Sjollema, K. A., Deckers, M., Erdmann, R., Marten Veenhuis, A., & van der Klei, I. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.03166 · Cited by 200
The peroxisome: still a mysterious organelle
Schrader, M., & Fahimi, H. D. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0396-9 · Cited by 207
Fission and proliferation of peroxisomes
Schrader, M., Bonekamp, N. A., & Islinger, M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.014 · Cited by 189
Zerihun, M., Sukumaran, S., & Qvit, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065785 · Cited by 198
Mechanisms Orchestrating Mitochondrial Dynamics for Energy Homeostasis
Yu, S. B., & Pekkurnaz, G. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.07.027 · Cited by 184
Morphological dynamics of mitochondria — A special emphasis on cardiac muscle cells
Hom, J., & Sheu, S. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.02.023 · Cited by 189
The different facets of organelle interplay—an overview of organelle interactions
Schrader, M., Godinho, L. F., Costello, J. L., & Islinger, M. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00056 · Cited by 181
Origin and evolution of the peroxisomal proteome
Gabaldón, T., Snel, ., van Zimmeren, F., Hemrika, W., Tabak, H. F., & Huynen, M. A. (2006) · Biology Direct · doi:10.1186/1745-6150-1-8 · Cited by 176
Dynamin‐related proteins and Pex11 proteins in peroxisome division and proliferation
Thoms, S., & Erdmann, R. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04939.x · Cited by 172
Dual role of USP30 in controlling basal pexophagy and mitophagy
Marcassa, E., Kallinos, A., Jardine, J., Rusilowicz‐Jones, E. V., Martinez, A., Kuehl, S., Islinger, M., Clague, M. J., & Urbé, S. (2018) · The EMBO Reports · doi:10.15252/embr.201745595 · Cited by 158
Koch, J., Pranjic, K., Huber, A., Ellinger, A., Hartig, A., Kragler, F., & Brocard, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.064907 · Cited by 163
Kemper, C., Habib, S. J., Engl, G., Heckmeyer, P., Dimmer, K. S., & Rapaport, D. (2008) · Journal of Cell Science · doi:10.1242/jcs.024034 · Cited by 161
Proliferation and fission of peroxisomes — An update
Schrader, M., Costello, J. L., Godinho, L. F., Azadi, A. S., & Islinger, M. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.09.024 · Cited by 170
Functional and morphological impact of ER stress on mitochondria
Vannuvel, K., Renard, P., Raes, M. J., & Arnould, T. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24360 · Cited by 161
Mitofusin 2: A Mitochondria-Shaping Protein with Signaling Roles Beyond Fusion
de Brito, O. M., & Scorrano, L. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1934 · Cited by 155
Platta, H. W., & Erdmann, R. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.06.009 · Cited by 152
Receptor-mediated Drp1 oligomerization on endoplasmic reticulum
Ji, W.-K., Chakrabarti, R., Fan, X., Schoenfeld, L. W., Strack, S., & Higgs, H. N. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201610057 · Cited by 151
Organelle interplay-peroxisome interactions in health and disease.
Schrader, M., Kamoshita, M., & Islinger, M. (2020) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12083 · Cited by 149
Self-citationFis1, DLP1, and Pex11p coordinately regulate peroxisome morphogenesis
Kobayashi, S., Tanaka, A., & Fujiki, Y. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.02.028 · Cited by 145
Multiple faces of dynamin-related protein 1 and its role in Alzheimer's disease pathogenesis
Kandimalla, R. J. L., & Reddy, P. H. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.12.018 · Cited by 148
Ergosterol content specifies targeting of tail-anchored proteins to mitochondrial outer membranes
Krumpe, K., Frumkin, I., Herzig, Y., Rimon, N., Özbalci, C., Brügger, B., Rapaport, D., & Schuldiner, M. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-12-0994 · Cited by 143
Mitochondria and peroxisomes: Are the ‘Big Brother’ and the ‘Little Sister’ closer than assumed?
Schrader, M., & Yoon, Y. (2007) · BioEssays · doi:10.1002/bies.20659 · Cited by 136
Peroxisome biogenesis in mammalian cells
Fujiki, Y., Okumoto, K., Mukai, S., Honsho, M., & Tamura, S. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00307 · Cited by 129
Mitochondrial-mediated antiviral immunity
Koshiba, T. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.03.005 · Cited by 134
Shared components of mitochondrial and peroxisomal division
Schrader, M. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.01.004 · Cited by 134
Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p
Motley, A. M., Ward, G. P., & Hettema, E. H. (2008) · Journal of Cell Science · doi:10.1242/jcs.026344 · Cited by 139
Ceramide induced mitophagy and tumor suppression
Dany, M., & Öğretmen, B. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.039 · Cited by 130
Mitochondrial Morphofunction in Mammalian Cells
Bulthuis, E. P., Adjobo-Hermans, M. J. W., Willems, P. H. G. M., & Koopman, W. J. H. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7534 · Cited by 133
Halbach, A., Landgraf, C., Lorenzen, S., Rosenkranz, K., Volkmer, R., Erdmann, R., & Rottensteiner, H. (2006) · Journal of Cell Science · doi:10.1242/jcs.02979 · Cited by 123
Peroxisome Biogenesis and Function
Kaur, N., Reumann, S., & Hu, J. (2009) · The Arabidopsis Book · doi:10.1199/tab.0123 · Cited by 128
A Perspective on Transport of Proteins into Mitochondria: A Myriad of Open Questions
Neupert, W. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.02.001 · Cited by 121
Clippinger, A. J., & Bouchard, M. J. (2008) · Journal of Virology · doi:10.1128/jvi.00154-08 · Cited by 121
Peroxisome biogenesis disorders
Argyriou, C., D’Agostino, D., & Braverman, N. (2016) · Translational Science of Rare Diseases · doi:10.3233/trd-160003 · Cited by 129
The control of peroxisome number and size during division and proliferation
Yan, M., Rayapuram, N., & Subramani, S. E. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.06.003 · Cited by 120
Ihenacho, U. K., Nolden, K. A., Harwig, M. C., Widlansky, M. E., & Hill, R. B. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.660095 · Cited by 117
Maintaining Peroxisome Populations: A Story of Division and Inheritance
Fagarasanu, A. D., Fagarasanu, M., & Rachubinski, R. A. (2007) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123456 · Cited by 118
ER as master regulator of membrane trafficking and organelle function
Wenzel, E. M., Elfmark, L. A., Stenmark, H., & Raiborg, C. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202205135 · Cited by 120
Zhao, Y., Sun, X., Hu, D., Prosdocimo, D. A., Hoppel, C. L., Jain, M. K., Ramachandran, R., & Qi, X. (2019) · Nature Communications · doi:10.1038/s41467-019-09291-x · Cited by 111
Dynamin Assembly Strategies and Adaptor Proteins in Mitochondrial Fission
Bui, H., & Shaw, J. M. (2013) · Current Biology · doi:10.1016/j.cub.2013.08.040 · Cited by 114
Peroxisome: Metabolic Functions and Biogenesis
Okumoto, K., Tamura, S., Honsho, M., & Fujiki, Y. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-60204-8_1 · Cited by 111
Mitochondrial Dynamics: The Intersection of Form and Function
Ferree, A. W., & Shirihai, O. S. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_2 · Cited by 113
Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells
Costello, J. L., Castro, I. G., Camões, F., Schrader, T. A., McNeall, D., Yang, J., Giannopoulou, E., Gomes, S. R. A. M., Pogenberg, V., Bonekamp, N. A., et al. (2017) · Journal of Cell Science · doi:10.1242/jcs.200204 · Cited by 115
Tail-anchored PEX26 targets peroxisomes via a PEX19-dependent and TRC40-independent class I pathway
Yagita, Y., Hiromasa, T., & Fujiki, Y. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201211077 · Cited by 99
Making two organelles from one: Woronin body biogenesis by peroxisomal protein sorting
Liu, F., Ng, S. K., Lu, Y., Low, W., Lai, J., & Jedd, G. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200705049 · Cited by 101
Insights into amyloid-β-induced mitochondrial dysfunction in Alzheimer disease
Wang, X., Su, B., Perry, G. L., Smith, M. A., & Zhu, X. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.09.007 · Cited by 102
Growth and Division of Peroxisomes
Schrader, M., & Fahimi, H. D. (2006) · International review of cytology · doi:10.1016/s0074-7696(06)55005-3 · Cited by 107
Lingard, M. J., Gidda, S. K., Bingham, S. E., Rothstein, S. J., Mullen, R. T., & Trelease, R. N. (2008) · The Plant Cell · doi:10.1105/tpc.107.057679 · Cited by 100
Chen, X., Zhang, Z., Li, H., Zhao, J., Wei, X., Lin, W., Zhao, X., Jiang, A., & Yuan, J. (2020) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.15027 · Cited by 96
Zhang, X., & Hu, J. (2008) · The Plant Journal · doi:10.1111/j.1365-313x.2008.03677.x · Cited by 97
Huber, N., Guimarães, S., Schrader, M., Suter, U., & Niemann, A. (2013) · EMBO Reports · doi:10.1038/embor.2013.56 · Cited by 94
Organelle dynamics and dysfunction: A closer link between peroxisomes and mitochondria
Camões, F., Bonekamp, N. A., Delille, H. K., & Schrader, M. (2008) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-008-1018-3 · Cited by 93
Nagotu, S., Saraya, R., Otzen, M., Marten Veenhuis, A., & van der Klei, I. J. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.10.018 · Cited by 89
Pex11pβ-mediated growth and division of mammalian peroxisomes follows a maturation pathway
Delille, H. K., Agricola, B., Guimarães, S., Borta, H., Lüers, G. H., Fransen, M., & Schrader, M. (2010) · Journal of Cell Science · doi:10.1242/jcs.062109 · Cited by 89
Desai, M., & Hu, J. (2008) · PLANT PHYSIOLOGY · doi:10.1104/pp.107.113555 · Cited by 87
PEX11 proteins attract Mff and hFis1 to coordinate peroxisomal fission
Koch, J., & Brocard, C. (2012) · Journal of Cell Science · doi:10.1242/jcs.102178 · Cited by 86
A role for Mitochondrial Rho GTPase 1 (MIRO1) in motility and membrane dynamics of peroxisomes
Castro, I. G., Richards, D. M., Metz, J., Costello, J. L., Passmore, J. B., Schrader, T. A., Gouveia, A., Ribeiro, D., & Schrader, M. (2018) · Traffic · doi:10.1111/tra.12549 · Cited by 91
Mitochondrial dynamics, cell death and the pathogenesis of Parkinson’s disease
Büeler, H. (2010) · APOPTOSIS · doi:10.1007/s10495-010-0465-0 · Cited by 87
Mitofusin 2 as a Driver That Controls Energy Metabolism and Insulin Signaling
Antonio Zorzano, A., Hernández‐Álvarez, M. I., Sebastián, D., & Muñoz, J. P. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6208 · Cited by 83
Peroxisome Formation and Maintenance Are Dependent on the Endoplasmic Reticulum
Tabak, H. F., Braakman, I., & van der Zand, A. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-081111-125123 · Cited by 82
Zhong, K., Xiao, L., Xinyi, L., Kong, X., Zhang, H., Zheng, X., Wang, P., & Zhang, Z. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005823 · Cited by 84
Redox regulation of UPR signalling and mitochondrial ER contact sites
Casas-Martinez, J. C., Samali, A., & McDonagh, B. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05286-0 · Cited by 85
Peroxisome Interactions and Cross-Talk with Other Subcellular Compartments in Animal Cells
Schrader, M., Grille, S., Fahimi, H. D., & Islinger, M. (2013) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-6889-5_1 · Cited by 82
FISSION1A and FISSION1B Proteins Mediate the Fission of Peroxisomes and Mitochondria in Arabidopsis
Zhang, X., & Hu, J. (2008) · Molecular Plant · doi:10.1093/mp/ssn056 · Cited by 78
Sulforaphane is a Nrf2-independent inhibitor of mitochondrial fission
O'Mealey, G. B., Berry, W. L., & Plafker, S. M. (2016) · Redox Biology · doi:10.1016/j.redox.2016.11.007 · Cited by 79
Emerging roles of mitochondria in the evolution, biogenesis, and function of peroxisomes
Mohanty, A., & McBride, H. M. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00268 · Cited by 76
Discovery of the membrane receptor for mitochondrial fission GTPase Drp1
Otera, H., & Mihara, K. (2011) · Small GTPases · doi:10.4161/sgtp.2.3.16486 · Cited by 78
Metadata
- Authors
- Koch, A., Yoon, Y., Bonekamp, N. A., McNiven, M. A., & Schrader, M.
- Affiliations
- Philipps University of Marburg (DE)
- University of Rochester Medicine (US)
- Mayo Clinic (US)
- Venue
- Molecular Biology of the Cell
- Published
- 2005-11
- Volume
- 16
- Issue
- 11
- Pages
- 5077-5086
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC1266408
- OpenAlex
- W2128023952
- Cited by
- 308
- References
- 42
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 13 · 2023: 13 · 2022: 16 · 2021: 8 · 2020: 17 · 2019: 10 · 2018: 17 · 2017: 11 · 2016: 15 · 2015: 17 · 2014: 14 · 2013: 24 · 2012: 15
- FWCI
- 6.42
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Philipps-Universität Marburg
- La Trobe University
- Universität Heidelberg
- Université de Genève
- 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 › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- Fis1, mitochondrial fission, Drp1, dynamin-like protein, peroxisome division, peroxisome targeting, transmembrane domain, C-terminal tail, mammalian cells
- MeSH terms
- Animals, Chlorocebus aethiops, Humans, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Transfection, COS Cells, GTP Phosphohydrolases, Peroxisomes, Mitochondrial Proteins, Dynamins, RNA, Small Interfering, Cell Line, Tumor, Rats
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