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Newly born peroxisomes are a hybrid of mitochondrial and ER-derived pre-peroxisomes
Abstract
Peroxisomes function together with mitochondria in a number of essential biochemical pathways, from bile acid synthesis to fatty acid oxidation. Peroxisomes grow and divide from pre-existing organelles, but can also emerge de novo in the cell. The physiological regulation of de novo peroxisome biogenesis remains unclear, and it is thought that peroxisomes emerge from the endoplasmic reticulum in both mammalian and yeast cells. However, in contrast to the yeast system, a number of integral peroxisomal membrane proteins are imported into mitochondria in mammalian cells in the absence of peroxisomes, including Pex3, Pex12, Pex13, Pex14, Pex26, PMP34 and ALDP. Overall, the mitochondrial localization of peroxisomal membrane proteins in mammalian cells has largely been considered a mis-targeting artefact in which de novo biogenesis occurs exclusively from endoplasmic reticulum-targeted peroxins. Here, in following the generation of new peroxisomes within human patient fibroblasts lacking peroxisomes, we show that the essential import receptors Pex3 and Pex14 target mitochondria, where they are selectively released into vesicular pre-peroxisomal structures. Maturation of pre-peroxisomes containing Pex3 and Pex14 requires fusion with endoplasmic reticulum-derived vesicles carrying Pex16, thereby providing full import competence. These findings demonstrate the hybrid nature of newly born peroxisomes, expanding their functional links to mitochondria.
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“Peroxisomes have recently been shown to have a shared mitochondrial and endoplasmic reticulum (ER) origin, further linking the function of mitochondria and peroxisomes (Sugiura et al., 2017).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Sugiura et al., 2017
In the citing paper
“In de novo synthesis, mature peroxisomes are built incrementally, with the first step a budding of pre-peroxisomal vesicles bearing complementary proteins of the early import machinery, PEX16 and PEX3, from membranes of the endoplasmic reticulum and mitochondria, respectively (Schrader and Pellegrini, 2017; Sugiura et al., 2017). Heterotypic fusion of PEX3- and PEX16-bearing vesicles establish a”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Sugiura et al., 2017
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Cites
Lazarow, P. B., & Fujiki, Y. (1985) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.01.110185.002421 · Cited by 1,114
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
Self-citationA Vesicular Transport Pathway Shuttles Cargo from Mitochondria to Lysosomes
Soubannier, V., McLelland, G., Zunino, R., Braschi, E., Rippstein, P. U., Fon, E. A., & McBride, H. M. (2012) · Current Biology · doi:10.1016/j.cub.2011.11.057 · Cited by 755
Self-citation[6] Preparation of microsomal membranes for cotranslational protein translocation
Walter, P., & Blobel, G. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(83)96010-x · Cited by 656
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
Self-citationSmith, J. J., & Aitchison, J. D. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3700 · Cited by 470
Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence.
Nguyen, M., Millar, D. G., Yong, V. W., Korsmeyer, S. J., & Shore, G. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74386-5 · Cited by 393
GEF-H1 Couples Nocodazole-induced Microtubule Disassembly to Cell Contractility via RhoA
Chang, Y.-C., Nalbant, P., Birkenfeld, J., Chang, Z.-F., & Bokoch, G. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1269 · Cited by 377
Kim, P. K., Mullen, R. T., Schümann, U., & Lippincott‐Schwartz, J. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601036 · Cited by 344
Sacksteder, K. A., Jones, J. M., South, S. T., Li, X., Liu, Y., & Gould, S. J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.5.931 · Cited by 312
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A glossary of plant cell structures: Current insights and future questions
Kang, B., Anderson, C. T., Arimura, S., Bayer, E., Bezanilla, M., Botella, M. A., Brandizzí, F., Burch‐Smith, T. M., Chapman, K. D., Dünser, K., et al. (2021) · The Plant Cell · doi:10.1093/plcell/koab247 · Cited by 55
In defence of the three-domains of life paradigm
van der Gulik, P. T. S., Hoff, W. D., & Speijer, D. (2017) · BMC Evolutionary Biology · doi:10.1186/s12862-017-1059-z · Cited by 53
“with (pre)mitochondrial fatty acid oxidation [18, 19].”
Almeida, C., & Amaral, M. D. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03523-w · Cited by 51
Plant peroxisomal solute transporter proteins
Charton, L., Plett, A., & Linka, N. (2019) · Journal of Integrative Plant Biology · doi:10.1111/jipb.12790 · Cited by 53
Extramitochondrial cardiolipin suggests a novel function of mitochondria in spermatogenesis
Ren, M., Xu, Y., Erdjument‐Bromage, H., Donelian, A., Phoon, C. K. L., Terada, N., Strathdee, D., Neubert, T. A., & Schlame, M. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201808131 · Cited by 51
“For instance, mitochondria have been recognized as the precursor of the nebenkern in insect sperm (Perry et al., 1959), and they have been implicated in the assembly of peroxisomes (Sugiura et al., 2017).”
Peroxisomal fission is modulated by the mitochondrial Rho‐GTPases, Miro1 and Miro2
Covill‐Cooke, C., Toncheva, V. S., Drew, J., Birsa, N., López‐Doménech, G., & Kittler, J. T. (2020) · EMBO Reports · doi:10.15252/embr.201949865 · Cited by 53
“Peroxisomal fission also serves as an important mechanism of peroxisomal biogenesis along-side de novo formation, the combination of pre-peroxisomal vesicles from the endoplasmic reticulum and mitochondria [3 – 5].”
Rapid affinity purification of intracellular organelles using a twin strep tag
Xiong, J., He, J., Xie, W. P., Hinojosa, E., Ambati, C. R., Putluri, N., Kim, H.-E., Zhu, M. X., & Du, G. (2019) · Journal of Cell Science · doi:10.1242/jcs.235390 · Cited by 49
“, 2016); (2) new peroxisomes are partially derived from mitochondria and therefore mitochondria and peroxisomes carry some common proteins (Sugiura et al., 2017); (3) SLC27A2 is absent in the purified mitochondria (Fig.”
BackgroundMethodPlasmalogen loss caused by remodeling deficiency in mitochondria
Kimura, T., Kimura, A. K., Ren, M., Monteiro, V., Xu, Y., Berno, B., Schlame, M., & Epand, R. M. (2019) · Life Science Alliance · doi:10.26508/lsa.201900348 · Cited by 49
“The fact, however, that the de novo formation of peroxisomes is initiated by budding off preperoxisomal vesicles from mitochondria (Sugiura et al, 2017), which is damaged in BTHS, as well as from the ER led us to look into the level of peroxisomes.”
BackgroundMethodThe Emerging Role of RHOT1/Miro1 in the Pathogenesis of Parkinson's Disease
Großmann, D., Berenguer-Escuder, C., Chemla, A., Arena, G., & Krüger, R. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.00587 · Cited by 55
“The physical link to mitochondria and the ER is important for peroxisomal proliferation and function (139, 140).”
BackgroundMolecular insights into peroxisome homeostasis and peroxisome biogenesis disorders
Fujiki, Y., Okumoto, K., Honsho, M., & Abe, Y. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119330 · Cited by 47
Intracellular to Interorgan Mitochondrial Communication in Striated Muscle in Health and Disease
Boardman, N. T., Trani, G., Scalabrin, M., Romanello, V., & Wüst, R. C. I. (2023) · Endocrine Reviews · doi:10.1210/endrev/bnad004 · Cited by 51
Quantitative subcellular reconstruction reveals a lipid mediated inter-organelle biogenesis network
Lee, R. G., Rudler, D. L., Raven, S. A., Peng, L., Chopin, A., Moh, E. S. X., McCubbin, T., Siira, S. J., Fagan, S. V., DeBono, N. J., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01297-4 · Cited by 49
“Inter-organelle communication is driven by membrane-bound vesicles 11,35 ; we therefore analysed the total membrane volume of vesicles and found that their interactions with mitochondria were decreased in the KO cell lines (Fig.”
Peroxisomes: role in cellular ageing and age related disorders
Deori, N. M., Kale, A., Maurya, P. K., & Nagotu, S. (2018) · Biogerontology · doi:10.1007/s10522-018-9761-9 · Cited by 47
Cichocki, B. A., Krumpe, K., Vitali, D. G., & Rapaport, D. (2018) · Traffic · doi:10.1111/tra.12604 · Cited by 47
“Recently, a study in mammalian cells demonstrated that the peroxisomal proteins Pex14 and the Pex19 receptor Pex3 are partially targeted to mitochondria and can induce there formation of mitochondria derived preperoxisomes.(65) However, so far, Pex3 was not found in yeast mitochondria.”
BackgroundPexophagy in yeast and mammals: an update on mysteries
Eberhart, T., & Kovacs, W. J. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1724-3 · Cited by 46
Lismont, C., Koster, J., Provost, S., Baes, M. I., Veldhoven, P. P. V., Waterham, H. R., & Fransen, M. (2019) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2019.05.013 · Cited by 48
Mitochondrial Dynamics at Different Levels: From Cristae Dynamics to Interorganellar Cross Talk
Kondadi, A. K., & Reichert, A. S. (2024) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-030822-020736 · Cited by 46
Fatty Liver Due to Increased de novo Lipogenesis: Alterations in the Hepatic Peroxisomal Proteome
Knebel, B., Fahlbusch, P., Dille, M. A., Wahlers, N., Hartwig, S., Jacob, S., Kettel, U., Schiller, M., Herebıan, D., Koellmer, C., et al. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00248 · Cited by 44
“It has been shown that this is a more complex process, including the development of pre-peroxisomes originated from mitochondria, which fuse with endoplasmic vesicles from the ER for maturation by a PEX3 cycling process (Sugiura et al., 2017).”
BackgroundStaying in Healthy Contact: How Peroxisomes Interact with Other Cell Organelles
Sargsyan, Y., & Thoms, S. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.09.012 · Cited by 47
Deubiquitinating Enzymes Related to Autophagy: New Therapeutic Opportunities?
Jacomin, A., Taillebourg, E., & Fauvarque, M. (2018) · Cells · doi:10.3390/cells7080112 · Cited by 44
“Moreover, contact sites between mitochondria and peroxisomes exist, and mitochondria were shown to play a role in the generation of peroxisomes [114]; thus reinforcing the hypothesis of an intrinsic relationship between both organelles.”
BackgroundCan All Major ROS Forming Sites of the Respiratory Chain Be Activated By High FADH 2 /NADH Ratios?
Speijer, D. (2018) · BioEssays · doi:10.1002/bies.201800180 · Cited by 44
Yeast peroxisomes: How are they formed and how do they grow?
Akşit, A., & van der Klei, I. J. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.09.019 · Cited by 41
Miro proteins and their role in mitochondrial transfer in cancer and beyond
Nahácka, Z., Novák, J., Zobalová, R., & Neužil, J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.937753 · Cited by 41
“Here mitochondria can establish functional connection with recipient cellular organelles like the nucleus, ER or peroxisomes (Sugiura et al., 2017; Castro et al., 2018; Okumoto et al., 2018; Modi et al., 2019; Desai et al., 2020).”
BackgroundHuang, D., Chen, S., Xiong, D., Wang, H., Zhu, L., Wei, Y., Li, Y., & Zou, S. (2023) · Aging and Disease · doi:10.14336/ad.2023.0201 · Cited by 46
“Under certain conditions, mitochondria (and possibly the ER) also contribute to peroxisome biogenesis ( de novo formation) [151].”
BackgroundLocation is everything: protein translocations as a viral infection strategy
Cook, K. C., & Cristea, I. M. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.09.021 · Cited by 42
“Additionally, protein movement is required for the formation and maintenance of some organelles, like autophagosomes [8], mitochondria [9 ,10 ], and peroxisomes [11].”
BackgroundRole of lipids in interorganelle communication
Domingues, N. S., Pires, J., Milošević, I., & Raimundo, N. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.04.008 · Cited by 46
Lipid Droplet and Peroxisome Biogenesis: Do They Go Hand-in-Hand?
Joshi, A. S., & Cohen, S. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00092 · Cited by 38
“These PPVs fuse to form a functional peroxisome (Sugiura et al., 2017).”
BackgroundRobertson, G. L., Riffle, S., Patel, M., Bodnya, C., Marshall, A. G., Beasley, H. K., Lopez, E. G., Shao, J., Vue, Z., Hinton, A. O., Jr., et al. (2023) · Journal of Cell Science · doi:10.1242/jcs.260370 · Cited by 37
Hu, D., Tan, M., Lu, D., Kleiboeker, B. A., Liu, X., Park, H., Kravitz, A. V., Shoghi, K. I., Tseng, Y., Razani, B., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41849-8 · Cited by 41
“Since de novo formation of peroxisomes involves fusion of pre-peroxisomalvesicles derived from the ER and mitochondria 51 , it is conceivable that the increased mitochondrial localizationofTMEM135duringmitochondrial fi ssionre fl ectsfusionof peroxisomal membrane with mitochondria.”
Evolution of peroxisomes illustrates symbiogenesis
Speijer, D. (2017) · BioEssays · doi:10.1002/bies.201700050 · Cited by 38
“Recent findings: Mitochondrial membranes are involved in biogenesis of peroxisomes Last, but certainly not least, the group of McBride just published their surprising finding: In human fibroblasts without peroxisomes, peroxisomal import receptors Pex3 and Pex14 end up in mitochondria to be released in preperoxisomal v…”
BackgroundInfluentialSymbiogenesis, gradualism, and mitochondrial energy in eukaryote origin
Martin, W. F. (2017) · Periodicum Biologorum · doi:10.18054/pb.v119i3.5694 · Cited by 38
Multi-localized Proteins: The Peroxisome-Mitochondria Connection
Costello, J. L., Passmore, J. B., Islinger, M., & Schrader, M. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-13-2233-4_17 · Cited by 39
Passmore, J. B., Pinho, S., Gómez-Lázaro, M., & Schrader, M. (2017) · Histochemistry and Cell Biology · doi:10.1007/s00418-017-1577-1 · Cited by 38
“…of the membrane fission machineries (reviewed in Schrader et al. 2012, 2016), cooperate in anti-viral signalling (Dixit et al. 2010; Odendall et al. 2014) and may depend on each other for biogenesis and functionality (Peeters et al. 2011, 2015; Mohanty and McBride 2013; Sugiura et al. 2017).”
BackgroundPeroxisomal Membrane Contact Sites in Mammalian Cells
Chen, C., Li, J., Qin, X., & Wang, W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00512 · Cited by 39
Peroxisomal homeostasis in metabolic diseases and its implication in ferroptosis
Han, J., Zheng, D., Liu, P.-S., Wang, S., & Xie, X. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01862-w · Cited by 37
“Fusion of these vesicles leads to mature peroxisomes [50].”
BackgroundSubstantial Decrease in Plasmalogen in the Heart Associated with Tafazzin Deficiency
Kimura, T., Kimura, A. K., Ren, M., Berno, B., Xu, Y., Schlame, M., & Epand, R. M. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00042 · Cited by 36
Wāng, Y. (2024) · Environment International · doi:10.1016/j.envint.2024.109193 · Cited by 35
Mitochondrial fission – changing perspectives for future progress
Kamerkar, S. C., Liu, A., & Higgs, H. N. (2025) · Journal of Cell Science · doi:10.1242/jcs.263640 · Cited by 43
Peroxisomal ROS control cytosolic Mycobacterium tuberculosis replication in human macrophages
Pellegrino, E., Aylan, B., Bussi, C., Fearns, A., Bernard, E. M., Athanasiadi, N., Santucci, P., Botella, L., & Gutierrez, M. G. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202303066 · Cited by 35
“Moreover, in cells lacking peroxisomes, CAT mislocalized in the nucleus and cytosol of cells lacking peroxisomes, and PEX14 localized in TOM20 + structures, suggesting a relocalization into mitochondria as previously reported (Sugiura et al., 2017; Fig.”
Mitochondrial derived vesicles‐ Quo Vadis?
Ben-Menachem, R. H., Pines, O., & Saada, A. (2024) · The FEBS Journal · doi:10.1111/febs.17103 · Cited by 33
“The recruitment of additional extra-mitochondrial proteins cannot be excluded as peroxisomal proteins may be targeted to mitochondria in mammalian cells and could subsequently find their way into MDVs [38].”
Peroxisome prognostications: Exploring the birth, life, and death of an organelle
Mast, F. D., Rachubinski, R. A., & Aitchison, J. D. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201912100 · Cited by 33
Biase, I. D., Tortorelli, S., Kratz, L. E., Steinberg, S. J., Cusmano‐Ozog, K. P., & Braverman, N. (2019) · Genetics in Medicine · doi:10.1038/s41436-019-0713-9 · Cited by 35
“are required to form new peroxisome membranes from the endoplasmic reticulum and from mitochondrial membranes.(39) PEX11 (there are 3 isoforms, PEX11 alpha, beta,(40)”
BackgroundPeroxisome Biogenesis: A Union between Two Organelles
Kim, P. (2017) · Current Biology · doi:10.1016/j.cub.2017.02.052 · Cited by 33
Wanders, R. J. A. (2018) · Molecular and Cellular Probes · doi:10.1016/j.mcp.2018.02.001 · Cited by 33
Signaling and Regulation Through the NAD + and NADP + Networks
Hassinen, I. E. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7479 · Cited by 30
“In the absence of pre-peroxisomes, the peroxins are mistargeted into MOM (145).”
Choi, Y. B., Choi, Y., & Harhaj, E. W. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007058 · Cited by 30
“In the de novo peroxisomal biogenesis model, PEX19 shuttles the PMPs together with the membrane import receptors PEX3 and PEX16 through the generation of pre-peroxisomal vesicles that originate from the endoplasmic reticulum (ER) and mitochondria [50, 51].”
Speijer, D., Hammond, M., & Lukeš, J. (2020) · mBio · doi:10.1128/mbio.00955-20 · Cited by 31
“Peroxisomes are most easily understood as eukaryotic inventions to lower mitochondrial ROS formation (24), and recent findings strongly suggest that they developed specifically in response to the entry and incorporation of the premitochondrion (65, 66).”
BackgroundPerspectives on Organelle Interaction, Protein Dysregulation, and Cancer Disease
Díaz, P., Sandoval, A., Bravo, R., Quest, A. F. G., & Lavandero, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.613336 · Cited by 31
Ghzaiel, I., Zarrouk, A., Essadek, S., Martine, L., Hammouda, S., Yammine, A., Ksila, M., Nury, T., Meddeb, W., Tahri-Joutey, M., et al. (2022) · Steroids · doi:10.1016/j.steroids.2022.109032 · Cited by 32
Calle, X., Garrido‐Moreno, V., Lopez‐Gallardo, E., Norambuena‐Soto, I., Martínez, D., Peñaloza‐Otárola, A., Troncossi, A., Guerrero‐Moncayo, A., Ortega, A., Maracaja‐Coutinho, V., et al. (2022) · IUBMB Life · doi:10.1002/iub.2657 · Cited by 32
“Although no specific functions have been attributed to MUL1 in the peroxisome, mitochondriaderived vesicles are an essential substrate source for peroxisome synthesis.(14) Thus, the role of MUL1 in peroxisome function remains to be explored.”
BackgroundDFCP1 associates with lipid droplets
Gao, G., Sheng, Y., Yang, H., Chua, B. T., & Xu, L. M. (2019) · Cell Biology International · doi:10.1002/cbin.11199 · Cited by 29
Dynamic Regulation of Peroxisomes and Mitochondria during Fungal Development
Navarro-Espíndola, R., Suaste-Olmos, F., & Peraza‐Reyes, L. (2020) · Journal of Fungi · doi:10.3390/jof6040302 · Cited by 30
“Moreover, peroxisome biogenesis relies on mitochondrial-derived vesicles, which fuse with vesicles originated on the endoplasmic reticulum (ER) to produce peroxisome precursors, competent to develop into mature peroxisomes [24].”
BackgroundDegradative tubular lysosomes link pexophagy to starvation and early aging in C. elegans
Dolese, D. A., Junot, M. P., Ghosh, B., Butsch, T. J., Johnson, A. E., & Bohnert, K. A. (2021) · Autophagy · doi:10.1080/15548627.2021.1990647 · Cited by 32
“It is well-accepted that peroxisomes can form de novo [2,5].”
BackgroundPeroxisomal targeting of a protein phosphatase type 2C via mitochondrial transit
Stehlik, T., Kremp, M., Kahnt, J., Bölker, M., & Freitag, J. (2020) · Nature Communications · doi:10.1038/s41467-020-16146-3 · Cited by 28
Castro‐Sepúlveda, M., Fernández‐Verdejo, R., Tuñón‐Suárez, M., Morales‐Zúñiga, J., Troncoso, M. F., Jannas-Vela, S., & Zbinden‐Foncea, H. (2021) · The FASEB Journal · doi:10.1096/fj.202002615rr · Cited by 28
Distribution and Evolution of Peroxisomes in Alveolates (Apicomplexa, Dinoflagellates, Ciliates)
Ludewig-Klingner, A.-K., Michael, V., Jarek, M., Brinkmann, H., & Petersen, J. (2017) · Genome Biology and Evolution · doi:10.1093/gbe/evx250 · Cited by 28
“…model is supported by the observation that the beta-oxidation pathway in peroxisomes is derived from the mitochondrial one (Bolte et al. 2015) and the recent finding that the peroxisomal membrane partially derives from the mitochondrial membrane during peroxisomal biogenesis (Sugiura et al. 2017).”
BackgroundMiro GTPase domains regulate the assembly of the mitochondrial motor–adaptor complex
Davis, K., Basu, H., Izquierdo, I., Shurberg, E., & Schwarz, T. L. (2022) · Life Science Alliance · doi:10.26508/lsa.202201406 · Cited by 27
The Overlooked Transformation Mechanisms of VLCFAs: Peroxisomal β-Oxidation
Lu, Q., Zong, W., Zhang, M., Chen, Z., & Yang, Z. (2022) · Agriculture · doi:10.3390/agriculture12070947 · Cited by 26
How neurons maintain their axons long-term: an integrated view of axon biology and pathology
Smith, G. A., Sweeney, S. T., O’Kane, C. J., & Prokop, A. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1236815 · Cited by 28
“They can be formed de novo through the fusion of ER- and mitochondria-derived pre-peroxisomes, concurrent with the import of matrix proteins that contain peroxisomal targeting signals (‘12’ in Figure 1 >b/l; Kim, 2017; Sugiura et al., 2017; Fujiki et al., 2020).”
BackgroundThe making of a mammalian peroxisome, version 2.0: mitochondria get into the mix
Schrader, M., & Pellegrini, L. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.23 · Cited by 26
“such as pre-peroxisomes.(1) It is from this starting point that Sugiura et al.”
BackgroundInfluentialMitochatting – If only we could be a fly on the cell wall
Eisenberg‐Bord, M., & Schuldiner, M. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.04.012 · Cited by 28
Proteomic Profiling of Leishmania donovani Promastigote Subcellular Organelles
Jardim, A., Hardie, D. B., Boitz, J. M., & Borchers, C. H. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00817 · Cited by 26
Organelle size scaling over embryonic development
Wesley, C. C., Mishra, S., & Levy, D. L. (2020) · Wiley Interdisciplinary Reviews Developmental Biology · doi:10.1002/wdev.376 · Cited by 27
Rosy Beginnings: Studying Peroxisomes in Drosophila
Pridie, C., Ueda, K., & Simmonds, A. J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00835 · Cited by 27
Roberts, R. F., Bayne, A. N., Goiran, T., Lévesque, D., Boisvert, F., Trempe, J., & Fon, E. A. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00506 · Cited by 26
Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis
Judy, R. M., Sheedy, C. J., & Gardner, B. M. (2022) · Cells · doi:10.3390/cells11132067 · Cited by 24
“Mammalian cells undergoing de novo peroxisome biogenesis similarly generate distinct ppV populations by trafficking a set of PMPs to the ER and a distinct set to the mitochondrial outer membrane [30].”
BackgroundMitochondria-derived vesicles and their potential roles in kidney stone disease
Chaiyarit, S., & Thongboonkerd, V. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04133-3 · Cited by 27
“Similarly, MDVs containing peroxisomal biogenesis factor 3 (Pex3) and peroxisomal biogenesis factor 14 (Pex14) play crucial roles in peroxisomal biogenesis [92, 93].”
BackgroundMolecular Basis of Mitochondrial and Peroxisomal Division Machineries
Imoto, Y., Itoh, K., & Fujiki, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155452 · Cited by 27
Jiang, S., Uddin, M. J., Yu, X., Piao, L., Dorotea, D., Oh, G. T., & Ha, H. (2022) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2021.0274 · Cited by 25
“De novo biogenesis requires the fusion of two pre-peroxisomal vesicles, one from the endoplasmic reticulum (ER) and the other from mitochondria [10].”
BackgroundRegulation of peroxisomal trafficking and distribution
Covill-Cooke, C., Toncheva, V. S., & Kittler, J. T. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03687-5 · Cited by 29
Dai, J., Li, Y., Kametani, F., Cui, X., Igarashi, Y., Huo, J., Miyahara, H., Mori, M., & Higuchi, K. (2021) · eLife · doi:10.7554/elife.63538 · Cited by 24
“…11 of 19 the central metabolic role, it was shown that peroxisomes interact with many organelles involved in cellular lipid metabolism, such as the ER, mitochondria, lysosomes, and lipid droplets (Schrader et al., 2015; Wanders et al., 2018; Sugiura et al., 2017).”
BackgroundMoog, D., Przyborski, J. M., & Maier, U. G. (2017) · Genome Biology and Evolution · doi:10.1093/gbe/evx231 · Cited by 23
Choo, C. Y. L., Wu, P., Yago, J. I., & Chung, K.-R. (2022) · Microbiological Research · doi:10.1016/j.micres.2022.127236 · Cited by 22
Bacterial Type II Secretion System and Its Mitochondrial Counterpart
Shaliutina-Loginova, A., Francetić, O., & Doležal, P. (2023) · mBio · doi:10.1128/mbio.03145-22 · Cited by 22
“mitochondrial outer membrane that may fuse with peroxisomes (54) or even serve as a basis for peroxisome biogenesis (55).”
BackgroundCoukos, R., Yao, D., Sánchez, M. I., Strand, E. T., Olive, M. E., Udeshi, N. D., Weissman, J. S., Carr, S. A., Bassik, M. C., & Ting, A. Y. (2021) · eLife · doi:10.7554/elife.69142 · Cited by 21
HuR-dependent SOD2 protein synthesis is an early adaptation to anchorage-independence
Kim, Y. S., Tang, P. W., Welles, J. E., Pan, W., Javed, Z., Elhaw, A. T., Mythreye, K., Kimball, S. R., & Hempel, N. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102329 · Cited by 23
Qiao, J., Wang, C., Chen, Y., Yu, S., Liu, Y., Yu, S., Jiang, L., Jin, C., Wang, X., Zhang, P., et al. (2023) · Antioxidants · doi:10.3390/antiox12040920 · Cited by 23
“The peroxisome is another organelle containing enzymes that degrade peroxides [43].”
BackgroundMammalian pexophagy at a glance
Bajdzienko, J., & Bremm, A. (2024) · Journal of Cell Science · doi:10.1242/jcs.259775 · Cited by 22
Bürgi, J., Ekal, L., & Wilmanns, M. (2021) · Traffic · doi:10.1111/tra.12785 · Cited by 21
Biogenesis and Function of Peroxisomes in Human Disease with a Focus on the ABC Transporter
Imanaka, T. (2019) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b18-00723 · Cited by 22
Kalel, V. C., Li, M., Gaussmann, S., Delhommel, F., Schäfer, A.-B., Tippler, B. G., Jung, M., Maier, R., Oeljeklaus, S., Schliebs, W., et al. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.07.015 · Cited by 21
Protein Quality Control at the Mitochondrial Surface
den Brave, F., Gupta, A., & Becker, T. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.795685 · Cited by 21
Biogenesis and metabolic homeostasis of trypanosomatid glycosomes: New insights and new questions
Michels, P. A. M., & Gualdrón‐López, M. (2022) · Journal of Eukaryotic Microbiology · doi:10.1111/jeu.12897 · Cited by 20
Reduced mitochondria provide an essential function for the cytosolic methionine cycle
Zítek, J., Füssy, Z., Treitli, S. C., Peña‐Diaz, P., Vaitová, Z., Zavadska, D., Harant, K., & Hampl, V. (2022) · Current Biology · doi:10.1016/j.cub.2022.10.028 · Cited by 20
Lin, T.-K., Lin, K.-J., Lin, K.-L., Liou, C.-W., Chen, S.-D., Chuang, Y.-C., Wang, P.-W., Chuang, J.-H., & Wang, T.-J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.607392 · Cited by 19
“who used a human fibroblast cell line lacking Pex3 obtained from a patient with Zellweger syndrome (Sugiura et al., 2017).”
MethodHorbay, R., Syrvatka, V. J., Bedzai, A. O., van der Merwe, M., Burger, D. E., & Beug, S. T. (2025) · Journal of Extracellular Vesicles · doi:10.1002/jev2.70192 · Cited by 21
“Double-membrane bound, low-density content TOM20-negative and PHD-positive MDVs have been observed in fumarate hydratase double knock-out mouse kidney cells, resembling MDVs formed via SNX9-dependent mechanisms (Zecchini et al. 2023; Sugiura et al. 2017).”
Mitochondrial proteotoxicity: implications and ubiquitin-dependent quality control mechanisms
Karbowski, M., Oshima, Y., & Verhoeven, N. A. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04604-8 · Cited by 21
Import and quality control of peroxisomal proteins
Rudowitz, M., & Erdmann, R. (2023) · Journal of Cell Science · doi:10.1242/jcs.260999 · Cited by 19
Mohanty, A., Zunino, R., Soubannier, V., & Dilipkumar, S. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30114 · Cited by 19
“A recent report from the laboratory of Heidi McBride (McGill University) has uncovered a role for mitochondria in the de novo biogenesis of peroxisomes in mammalian cells.(13) Although, such studies and earlier work in the lab have highlighted the functional role of MAPL in sumoylation of DRP1 but its direct associati…”
BackgroundColasante, C., Chen, J., Ahlemeyer, B., Bonilla-Martinez, R., Karnati, S., & Baumgart‐Vogt, E. (2017) · PLoS ONE · doi:10.1371/journal.pone.0183150 · Cited by 21
“A more recent publication proposes that in mammalian cells de novo peroxisomal biogenesis begins with the budding of PEX3-loaded pre-peroxisomal vesicles from the mitochondrion, followed by their maturation to peroxisomal vesicles in the ER [25].”
BackgroundUnloosing the Gordian knot of peroxisome formation
Costello, J. L., & Schrader, M. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.02.002 · Cited by 22
Fission Impossible (?)—New Insights into Disorders of Peroxisome Dynamics
Carmichael, R. E., Islinger, M., & Schrader, M. (2022) · Cells · doi:10.3390/cells11121922 · Cited by 21
“Peroxisomes can also form de novo under certain conditions, which involves the ER and mitochondria [20,21].”
BackgroundFundamental roles for inter-organelle communication in aging
Donahue, E. K. F., Ruark, E. M., & Burkewitz, K. (2022) · Biochemical Society Transactions · doi:10.1042/bst20220519 · Cited by 19
Chen, G., Gan, J., Wu, F., Zhou, Z., Duan, Z., Zhang, K., Wang, S., Jin, H., Li, Y., Zhang, C., et al. (2025) · European Heart Journal · doi:10.1093/eurheartj/ehaf032 · Cited by 19
Organelle zones in mitochondria
Shimizu, S. (2018) · The Journal of Biochemistry · doi:10.1093/jb/mvy068 · Cited by 18
Autophagy in the mammalian nervous system: a primer for neuroscientists
Suomi, F., & McWilliams, T. G. (2019) · Neuronal Signaling · doi:10.1042/ns20180134 · Cited by 18
Anaerobic peroxisomes in Mastigamoeba balamuthi
Le, T. C., Žárský, V., Nývltová, E., Rada, P., Harant, K., Vancová, M., Verner, Z., Hrdý, I., & Tachezy, J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1909755117 · Cited by 17
“More recently, mitochondria appeared to be directly involved in peroxisome biogenesis as a source of peroxisomal membranes and membrane proteins (14).”
BackgroundPrognostic role of PHYH for overall survival (OS) in clear cell renal cell carcinoma (ccRCC)
Qiu, Z., Zezhi, G., Lei, J., He, Q., Jin-yao, P., & Ying, A. (2021) · European journal of medical research · doi:10.1186/s40001-021-00482-1 · Cited by 17
Santos, H. J., & Nozaki, T. (2022) · Journal of Eukaryotic Microbiology · doi:10.1111/jeu.12923 · Cited by 17
Ubiquitin ligase MARCH5 controls the formation of mitochondria-derived pre-peroxisomes
Zheng, J., Chen, J., Cao, Z., Wu, K., Wang, J., Guo, Y., & Zhuang, M. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.09.029 · Cited by 17
Metadata
- Authors
- Sugiura, A., Mattie, S., Prudent, J., & McBride, H. M.
- Affiliations
- Montreal Neurological Institute and Hospital (CA)
- Corresponding author
- McBride, Heidi M.
- Venue
- Nature
- Published
- 2017-02-01
- Volume
- 542
- Issue
- 7640
- Pages
- 251-254
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2585343016
- Cited by
- 386
- References
- 38
- Citations by year
- 2026: 26 · 2025: 25 · 2024: 26 · 2023: 42 · 2022: 47 · 2021: 46 · 2020: 42 · 2019: 44 · 2018: 53 · 2017: 34
- FWCI
- 25.24
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- peroxisome biogenesis, PEX3, PEX14, PEX16, PEX12, PEX13, ALDP, peroxisomal membrane proteins, mitochondrial targeting, endoplasmic reticulum
- MeSH terms
- Peroxins, Bacterial Proteins, Organelle Biogenesis, Cell Line, Endoplasmic Reticulum, Fibroblasts, Humans, Intracellular Membranes, Lipoproteins, Luminescent Proteins, Membrane Proteins, Mitochondria, Repressor Proteins, Zellweger Syndrome, Peroxisomes, Protein Transport
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