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Journal articles on the topic 'Dynamin Related Protein 1 (Drp1)'

Author: Grafiati

Published: 6 September 2023

Last updated: 31 July 2025

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1

Perry, Heather M., Liping Huang, Rebecca J. Wilson, et al. "Dynamin-Related Protein 1 Deficiency Promotes Recovery from AKI." Journal of the American Society of Nephrology 29, no. 1 (2017): 194–206. http://dx.doi.org/10.1681/asn.2017060659.

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The proximal tubule epithelium relies on mitochondrial function for energy, rendering the kidney highly susceptible to ischemic AKI. Dynamin-related protein 1 (DRP1), a mediator of mitochondrial fission, regulates mitochondrial function; however, the cell-specific and temporal role of DRP1 in AKI in vivo is unknown. Using genetic murine models, we found that proximal tubule–specific deletion of Drp1 prevented the renal ischemia-reperfusion–induced kidney injury, inflammation, and programmed cell death observed in wild-type mice and promoted epithelial recovery, which associated with activation

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2

Breitzig, Mason T., Matthew D. Alleyn, Richard F. Lockey, and Narasaiah Kolliputi. "A mitochondrial delicacy: dynamin-related protein 1 and mitochondrial dynamics." American Journal of Physiology-Cell Physiology 315, no. 1 (2018): C80—C90. http://dx.doi.org/10.1152/ajpcell.00042.2018.

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The constant physiological flux of mitochondrial fission and fusion is inextricably tied to the maintenance of cellular bioenergetics and the fluidity of mitochondrial networks. Yet, the intricacies of this dynamic duo remain unclear in diseases that encompass mitochondrial dysregulation. Particularly, the role of the GTPase fission protein dynamin-related protein 1 (Drp1) is of profound interest. Studies have identified that Drp1 participates in complex signaling pathways, suggesting that the function of mitochondria in pathophysiology may extend far beyond energetics alone. Research indicate

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3

Ugarte-Uribe, Begoña, Hans-Michael Müller, Miki Otsuki, Walter Nickel, and Ana J. García-Sáez. "Dynamin-related Protein 1 (Drp1) Promotes Structural Intermediates of Membrane Division." Journal of Biological Chemistry 289, no. 44 (2014): 30645–56. http://dx.doi.org/10.1074/jbc.m114.575779.

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Drp1 is a dynamin-like GTPase that mediates mitochondrial and peroxisomal division in a process dependent on self-assembly and coupled to GTP hydrolysis. Despite the link between Drp1 malfunction and human disease, the molecular details of its membrane activity remain poorly understood. Here we reconstituted and directly visualized Drp1 activity in giant unilamellar vesicles. We quantified the effect of lipid composition and GTP on membrane binding and remodeling activity by fluorescence confocal microscopy and flow cytometry. In contrast to other dynamin relatives, Drp1 bound to both curved a

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4

Oliver, Darryll, and P. Reddy. "Dynamics of Dynamin-Related Protein 1 in Alzheimer’s Disease and Other Neurodegenerative Diseases." Cells 8, no. 9 (2019): 961. http://dx.doi.org/10.3390/cells8090961.

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The purpose of this article is to highlight the role of dynamin-related protein 1 (Drp1) in abnormal mitochondrial dynamics, mitochondrial fragmentation, autophagy/mitophagy, and neuronal damage in Alzheimer’s disease (AD) and other neurological diseases, including Parkinson’s, Huntington’s, amyotrophic lateral sclerosis, multiple sclerosis, diabetes, and obesity. Dynamin-related protein 1 is one of the evolutionarily highly conserved large family of GTPase proteins. Drp1 is critical for mitochondrial division, size, shape, and distribution throughout the neuron, from cell body to axons, dendr

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Strack, Stefan, Theodore J. Wilson, and J. Thomas Cribbs. "Cyclin-dependent kinases regulate splice-specific targeting of dynamin-related protein 1 to microtubules." Journal of Cell Biology 201, no. 7 (2013): 1037–51. http://dx.doi.org/10.1083/jcb.201210045.

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Fission and fusion reactions determine mitochondrial morphology and function. Dynamin-related protein 1 (Drp1) is a guanosine triphosphate–hydrolyzing mechanoenzyme important for mitochondrial fission and programmed cell death. Drp1 is subject to alternative splicing of three exons with previously unknown functional significance. Here, we report that splice variants including the third but excluding the second alternative exon (x01) localized to and copurified with microtubule bundles as dynamic polymers that resemble fission complexes on mitochondria. A major isoform in immune cells, Drp1-x01

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6

Mooli, Raja Gopal Reddy, Dhanunjay Mukhi, Zhonghe Chen, Nia Buckner, and Sadeesh K. Ramakrishnan. "An indispensable role for dynamin-related protein 1 in beige and brown adipogenesis." Journal of Cell Science 133, no. 18 (2020): jcs247593. http://dx.doi.org/10.1242/jcs.247593.

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ABSTRACTEmerging evidence indicates that proper mitochondrial dynamics are critical for adipocyte differentiation and functional thermogenic capacity. We found that the mitochondrial fission protein dynamin-related protein 1 (DRP1, also known as DNML1) is highly expressed in brown adipose tissue compared to expression in white adipose tissue, and these expression levels increase during brown adipocyte differentiation. Our results reveal that the inhibition of DRP1 using mdivi-1 mitigates beige adipocyte differentiation and differentiation-associated mitochondrial biogenesis. We found that DRP1

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Cheng, Wen-Yu, Kuan-Chih Chow, Ming-Tsang Chiao, Yi-Chin Yang, and Chiung-Chyi Shen. "Higher Levels of Dynamin-related Protein 1 are Associated with Reduced Radiation Sensitivity of Glioblastoma Cells." Current Neurovascular Research 17, no. 4 (2020): 446–63. http://dx.doi.org/10.2174/1567202617666200623123638.

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Background: Dynamin-related protein 1 (DRP1) is a GTPase involved in mitochondrial fission, mitochondrial protein import, and drug sensitivity, suggesting an association with cancer progression. This study was conducted to evaluate the prognostic significance of DRP1 in glioblastoma multiforme (GBM). Methods: DRP1 expression was measured by immunohistochemistry and Western blotting. Correlations between DRP1 expression and clinicopathological parameters were determined by statistical analysis. Differences in survival were compared using the log-rank test. DRP1 expression was detected in 87.2%

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8

Bian, Xiyun, Jingman Xu, Huanhuan Zhao, et al. "Zinc-Induced SUMOylation of Dynamin-Related Protein 1 Protects the Heart against Ischemia-Reperfusion Injury." Oxidative Medicine and Cellular Longevity 2019 (July 22, 2019): 1–11. http://dx.doi.org/10.1155/2019/1232146.

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Background. Zinc plays a role in mitophagy and protects cardiomyocytes from ischemia/reperfusion injury. This study is aimed at investigating whether SUMOylation of Drp1 is involved in the protection of zinc ion on cardiac I/R injury. Methods. Mouse hearts were subjected to 30 minutes of regional ischemia followed by 2 hours of reperfusion (ischemia/reoxygenation (I/R)). Infarct size and apoptosis were assessed. HL-1 cells were subjected to 24 hours of hypoxia and 6 hours of reoxygenation (hypoxia/reoxygenation (H/R)). Zinc was given 5 min before reperfusion for 30 min. SENP2 overexpression pl

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9

Ko, Huey-Jiun, Cheng-Yu Tsai, Shean-Jaw Chiou, et al. "The Phosphorylation Status of Drp1-Ser637 by PKA in Mitochondrial Fission Modulates Mitophagy via PINK1/Parkin to Exert Multipolar Spindles Assembly during Mitosis." Biomolecules 11, no. 3 (2021): 424. http://dx.doi.org/10.3390/biom11030424.

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Mitochondrial fission and fusion cycles are integrated with cell cycle progression. Here we first re-visited how mitochondrial ETC inhibition disturbed mitosis progression, resulting in multipolar spindles formation in HeLa cells. Inhibitors of ETC complex I (rotenone, ROT) and complex III (antimycin A, AA) decreased the phosphorylation of Plk1 T210 and Aurora A T288 in the mitotic phase (M-phase), especially ROT, affecting the dynamic phosphorylation status of fission protein dynamin-related protein 1 (Drp1) and the Ser637/Ser616 ratio. We then tested whether specific Drp1 inhibitors, Mdivi-1

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10

Yu, Rong, Tong Liu, Chenfei Ning, et al. "The phosphorylation status of Ser-637 in dynamin-related protein 1 (Drp1) does not determine Drp1 recruitment to mitochondria." Journal of Biological Chemistry 294, no. 46 (2019): 17262–77. http://dx.doi.org/10.1074/jbc.ra119.008202.

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Recruitment of the GTPase dynamin-related protein 1 (Drp1) to mitochondria is a central step required for mitochondrial fission. Reversible Drp1 phosphorylation has been implicated in the regulation of this process, but whether Drp1 phosphorylation at Ser-637 determines its subcellular localization and fission activity remains to be fully elucidated. Here, using HEK 293T cells and immunofluorescence, immunoblotting, RNAi, subcellular fractionation, co-immunoprecipitation assays, and CRISPR/Cas9 genome editing, we show that Drp1 phosphorylated at Ser-637 (Drp1pS637) resides both in the cytosol

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11

Tanner, Michael J., Jingli Wang, Rong Ying, et al. "Dynamin-related protein 1 mediates low glucose-induced endothelial dysfunction in human arterioles." American Journal of Physiology-Heart and Circulatory Physiology 312, no. 3 (2017): H515—H527. http://dx.doi.org/10.1152/ajpheart.00499.2016.

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Intensive glycemic regulation has resulted in an increased incidence of hypoglycemia. Hypoglycemic burden correlates with adverse cardiovascular complications and contributes acutely and chronically to endothelial dysfunction. Prior data indicate that mitochondrial dysfunction contributes to hypoglycemia-induced endothelial dysfunction, but the mechanisms behind this linkage remain unknown. We attempt to determine whether clinically relevant low-glucose (LG) exposures acutely induce endothelial dysfunction through activation of the mitochondrial fission process. Characterization of mitochondri

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12

Fealy, Ciaran E., Anny Mulya, Nicola Lai, and John P. Kirwan. "Exercise training decreases activation of the mitochondrial fission protein dynamin-related protein-1 in insulin-resistant human skeletal muscle." Journal of Applied Physiology 117, no. 3 (2014): 239–45. http://dx.doi.org/10.1152/japplphysiol.01064.2013.

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Defects in mitochondrial dynamics, the processes of fission, fusion, and mitochondrial autophagy, may contribute to metabolic disease including type 2 diabetes. Dynamin-related protein-1 (Drp1) is a GTPase protein that plays a central role in mitochondrial fission. We hypothesized that aerobic exercise training would decrease Drp1 Ser616 phosphorylation and increase fat oxidation and insulin sensitivity in obese (body mass index: 34.6 ± 0.8 kg/m2) insulin-resistant adults. Seventeen subjects performed supervised exercise for 60 min/day, 5 days/wk at 80–85% of maximal heart rate for 12 wk. Insu

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13

Yamamori, Tohru, Satoshi Ike, Tomoki Bo, et al. "Inhibition of the mitochondrial fission protein dynamin-related protein 1 (Drp1) impairs mitochondrial fission and mitotic catastrophe after x-irradiation." Molecular Biology of the Cell 26, no. 25 (2015): 4607–17. http://dx.doi.org/10.1091/mbc.e15-03-0181.

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Accumulating evidence suggests that mitochondrial dynamics is crucial for the maintenance of cellular quality control and function in response to various stresses. However, the role of mitochondrial dynamics in cellular responses to ionizing radiation (IR) is still largely unknown. In this study, we provide evidence that IR triggers mitochondrial fission mediated by the mitochondrial fission protein dynamin-related protein 1 (Drp1). We also show IR-induced mitotic catastrophe (MC), which is a type of cell death associated with defective mitosis, and aberrant centrosome amplification in mouse e

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14

Stepanyants, Natalia, Patrick J. Macdonald, Christopher A. Francy, Jason A. Mears, Xin Qi, and Rajesh Ramachandran. "Cardiolipin's propensity for phase transition and its reorganization by dynamin-related protein 1 form a basis for mitochondrial membrane fission." Molecular Biology of the Cell 26, no. 17 (2015): 3104–16. http://dx.doi.org/10.1091/mbc.e15-06-0330.

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Cardiolipin (CL) is an atypical, dimeric phospholipid essential for mitochondrial dynamics in eukaryotic cells. Dynamin-related protein 1 (Drp1), a cytosolic member of the dynamin superfamily of large GTPases, interacts with CL and functions to sustain the balance of mitochondrial division and fusion by catalyzing mitochondrial fission. Although recent studies have indicated a role for CL in stimulating Drp1 self-assembly and GTPase activity at the membrane surface, the mechanism by which CL functions in membrane fission, if at all, remains unclear. Here, using a variety of fluorescence spectr

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15

Ibayashi, Yuta, Nao Hasuzawa, Seiji Nomura, et al. "Mitochondrial fission is required for thermogenesis in brown adipose tissue." PLOS ONE 19, no. 12 (2024): e0312352. https://doi.org/10.1371/journal.pone.0312352.

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Brown adipose tissue (BAT) thermogenesis is pivotal for maintaining body temperature and energy balance. Mitochondrial morphology is dynamically controlled by a balance between fusion and fission, which is crucial for cell differentiation, response to metabolic insults, and heat production. Dynamin-related protein 1 (Drp1) is a key regulator of mitochondrial fission. This study investigates the role of Drp1 in BAT development and thermogenesis by generating Drp1-deficient mice. These mice were created by crossing Drp1 floxed mice with fatty acid-binding protein 4-Cre (aP2-Cre) transgenic mice,

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16

Zoheb, Mohammed, Tahmeen Jammel, Shaik Iqbal Ahmed, Safia Begum, Bushra, and Aleem Ahmed Khan. "Dynamin-related protein 1 expression as a non-invasive biomarker for mitochondrial dysfunction in Parkinson’s disease." Romanian Journal of Neurology 24, no. 2 (2025): 134–43. https://doi.org/10.37897/rjn.2025.2.14.

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Background. Parkinson's disease (PD) is a progressive neurodegenerative disorder characterized by dopaminergic neuron loss. Mitochondria-mediated mechanisms – including excessive fission, impaired fusion, defective mitophagy, and oxidative stress – contribute to its pathogenesis. However, the relationship between mitochondrial dynamics and PD progression remains poorly defined. Dynamin-related protein 1 (Drp1), a master regulator of mitochondrial fission, is implicated in neurodegeneration. This study assessed whether peripheral blood Drp1 gene expression reflects mitochondrial dysfunction in

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17

Nolden, Kelsey A., John M. Egner, Jack J. Collier, et al. "Novel DNM1L variants impair mitochondrial dynamics through divergent mechanisms." Life Science Alliance 5, no. 12 (2022): e202101284. http://dx.doi.org/10.26508/lsa.202101284.

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Imbalances in mitochondrial and peroxisomal dynamics are associated with a spectrum of human neurological disorders. Mitochondrial and peroxisomal fission both involve dynamin-related protein 1 (DRP1) oligomerisation and membrane constriction, although the precise biophysical mechanisms by which distinct DRP1 variants affect the assembly and activity of different DRP1 domains remains largely unexplored. We analysed four unreported de novo heterozygous variants in the dynamin-1-like gene DNM1L, affecting different highly conserved DRP1 domains, leading to developmental delay, seizures, hypotoni

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18

Macdonald, Patrick J., Natalia Stepanyants, Niharika Mehrotra, et al. "A dimeric equilibrium intermediate nucleates Drp1 reassembly on mitochondrial membranes for fission." Molecular Biology of the Cell 25, no. 12 (2014): 1905–15. http://dx.doi.org/10.1091/mbc.e14-02-0728.

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The GTPase dynamin-related protein 1 (Drp1) catalyzes mitochondrial division, but the mechanisms remain poorly understood. Much of what is attributed to Drp1’s mechanism of action in mitochondrial membrane fission parallels that of prototypical dynamin in endocytic vesicle scission. Unlike the case for dynamin, however, no lipid target for Drp1 activation at the mitochondria has been identified. In addition, the oligomerization properties of Drp1 have not been well established. We show that the mitochondria-specific lipid cardiolipin is a potent stimulator of Drp1 GTPase activity, as well as o

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19

Liu, Wei-Lun, Chia-Yang Li, Wei-Chung Cheng, et al. "High Mobility Group Box 1 Promotes Lung Cancer Cell Migration and Motility via Regulation of Dynamin-Related Protein 1." International Journal of Molecular Sciences 22, no. 7 (2021): 3628. http://dx.doi.org/10.3390/ijms22073628.

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High mobility group box 1 (HMGB1) has been demonstrated to promote the migration and invasion of non-small cell lung cancer (NSCLC). However, the mechanism of action of HMGB1 in regulating tumor mobility remains unclear. Therefore, we aimed to investigate whether HMGB1 affects mitochondria distribution and regulates dynamin-related protein 1 (DRP1)-mediated lamellipodia/filopodia formation to promote NSCLC migration. The regulation of mitochondrial membrane tension, dynamics, polarization, fission process, and cytoskeletal rearrangements in lung cancer cells by HMGB1 was analyzed using confoca

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Kalb, Ryan C., Geoffrey O. Nyabuto, Michael P. Morran, et al. "The Large GTPase Guanylate-Binding Protein-1 (GBP-1) Promotes Mitochondrial Fission in Glioblastoma." International Journal of Molecular Sciences 25, no. 20 (2024): 11236. http://dx.doi.org/10.3390/ijms252011236.

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Glioblastomas (aka Glioblastoma multiformes (GBMs)) are the most deadly of the adult brain tumors. Even with aggressive treatment, the prognosis is extremely poor. The large GTPase Guanylate-Binding Protein-1 (GBP-1) contributes to the poor prognosis of GBM by promoting migration and invasion. GBP-1 is substantially localized to the cytosolic side of the outer membrane of mitochondria in GBM cells. Because mitochondrial dynamics, particularly mitochondrial fission, can drive cell migration and invasion, the potential interactions between GBP-1 and mitochondrial dynamin-related protein 1 (Drp1)

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21

Jiang, Hui, Feng Chen, DianZe Song, Xiaoqin Zhou, Long Ren, and Mei Zeng. "Dynamin-Related Protein 1 Is Involved in Mitochondrial Damage, Defective Mitophagy, and NLRP3 Inflammasome Activation Induced by MSU Crystals." Oxidative Medicine and Cellular Longevity 2022 (October 25, 2022): 1–22. http://dx.doi.org/10.1155/2022/5064494.

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Excessive generation of reactive oxygen species (ROS) has great impacts on MSU crystal-induced inflammation. Drp1-dependent mitochondrial fission is closely associated with mitochondrial ROS levels. However, whether Drp1 signaling contributes to MSU crystal-induced inflammation remains unclear. Mice bone marrow-derived macrophages (BMDMs) were primed with LPS and then stimulated with MSU suspensions for 12 h. The protein levels associated with mitochondrial dynamics, oxidative stress, and mitophagy were detected by Western blot. BMDMs were loaded with MitoTracker Green probe to detect mitochon

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Horn, Sarah R., Michael J. Thomenius, Erika Segear Johnson, et al. "Regulation of mitochondrial morphology by APC/CCdh1-mediated control of Drp1 stability." Molecular Biology of the Cell 22, no. 8 (2011): 1207–16. http://dx.doi.org/10.1091/mbc.e10-07-0567.

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Homeostatic maintenance of cellular mitochondria requires a dynamic balance between fission and fusion, and controlled changes in morphology are important for processes such as apoptosis and cellular division. Interphase mitochondria have been described as an interconnected network that fragments as cells enter mitosis, and this mitotic mitochondrial fragmentation is known to be regulated by the dynamin-related GTPase Drp1 (dynamin-related protein 1), a key component of the mitochondrial division machinery. Loss of Drp1 function and the subsequent failure of mitochondrial division during mitos

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Fan, Kexia, Xiao Ding, Zhenle Zang, et al. "Drp1-Mediated Mitochondrial Metabolic Dysfunction Inhibits the Tumor Growth of Pituitary Adenomas." Oxidative Medicine and Cellular Longevity 2022 (March 23, 2022): 1–23. http://dx.doi.org/10.1155/2022/5652586.

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Metabolic changes have been suggested to be a hallmark of tumors and are closely associated with tumorigenesis. In a previous study, we demonstrated the role of lactate dehydrogenase in regulating abnormal glucose metabolism in pituitary adenomas (PA). As the key organelle of oxidative phosphorylation (OXPHOS), mitochondria play a vital role in the energy supply for tumor cells. However, few attempts have been made to elucidate mitochondrial metabolic homeostasis in PA. Dynamin-related protein 1 (Drp1) is a member of the dynamin superfamily of GTPases, which mediates mitochondrial fission. Thi

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Terrero, David, Amit Tiwari, and Dayanidhi Raman. "Abstract P1-13-12: Targeting Dynamin-related protein 1 for the management of taxane-resistant triple-negative breast cancer." Cancer Research 83, no. 5_Supplement (2023): P1–13–12—P1–13–12. http://dx.doi.org/10.1158/1538-7445.sabcs22-p1-13-12.

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Abstract The development of drug resistance is a primary cause of chemotherapy failure in the treatment of triple-negative breast cancer (TNBC). Some cancer cells are resistant to drugs with unrelated structures and mechanisms of action, a phenomenon known as multidrug resistance (MDR). Although taxanes such as docetaxel and paclitaxel are effective against non-metastatic and metastatic TNBC and other types of breast cancer, they eventually become ineffective due to development of drug resistance. Mitochondrial dynamics has gained significant attention as a means to treat MDR and non-MDR cance

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Han, Xiao-Jian, Yun-Fei Lu, Shun-Ai Li та ін. "CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology". Journal of Cell Biology 182, № 3 (2008): 573–85. http://dx.doi.org/10.1083/jcb.200802164.

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Mitochondria are dynamic organelles that frequently move, divide, and fuse with one another to maintain their architecture and functions. However, the signaling mechanisms involved in these processes are still not well characterized. In this study, we analyze mitochondrial dynamics and morphology in neurons. Using time-lapse imaging, we find that Ca2+ influx through voltage-dependent Ca2+ channels (VDCCs) causes a rapid halt in mitochondrial movement and induces mitochondrial fission. VDCC-associated Ca2+ signaling stimulates phosphorylation of dynamin-related protein 1 (Drp1) at serine 600 vi

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Park, Hong-Su, Guanqun Liu, Qiang Liu, and Yan Zhou. "Swine Influenza Virus Induces RIPK1/DRP1-Mediated Interleukin-1 Beta Production." Viruses 10, no. 8 (2018): 419. http://dx.doi.org/10.3390/v10080419.

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Nucleotide-binding domain and leucine-rich repeat-containing protein 3 (NLRP3) inflammasome plays a pivotal role in modulating lung inflammation in response to the influenza A virus infection. We previously showed that the swine influenza virus (SIV) infection induced NLRP3 inflammasome-mediated IL-1β production in primary porcine alveolar macrophages (PAMs), and we were interested in examining the upstream signaling events that are involved in this process. Here, we report that the SIV-infection led to dynamin-related protein 1 (DRP1) phosphorylation at serine 579 and mitochondrial fission in

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Losón, Oliver C., Zhiyin Song, Hsiuchen Chen, and David C. Chan. "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission." Molecular Biology of the Cell 24, no. 5 (2013): 659–67. http://dx.doi.org/10.1091/mbc.e12-10-0721.

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Several mitochondrial outer membrane proteins—mitochondrial fission protein 1 (Fis1), mitochondrial fission factor (Mff), mitochondrial dynamics proteins of 49 and 51 kDa (MiD49 and MiD51, respectively)—have been proposed to promote mitochondrial fission by recruiting the GTPase dynamin-related protein 1 (Drp1), but fundamental issues remain concerning their function. A recent study supported such a role for Mff but not for Fis1. In addition, it is unclear whether MiD49 and MiD51 activate or inhibit fission, because their overexpression causes extensive mitochondrial elongation. It is also unk

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Otasevic, Vesna, Lela Surlan, Milica Vucetic, et al. "Expression patterns of mitochondrial OXPHOS components, mitofusin 1 and dynamin-related protein 1 are associated with human embryo fragmentation." Reproduction, Fertility and Development 28, no. 3 (2016): 319. http://dx.doi.org/10.1071/rd13415.

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Developmental dysfunction in embryos, such as a lethal level of fragmentation, is assumed to be mitochondrial in origin. This study investigated the molecular basis of mitochondrial impairment in embryo fragmentation. Transcription patterns of factors that determine mitochondrial functionality: (i) components of the oxidative phosphorylation (OXPHOS) – complex I, cytochrome b, complex IV and ATP synthase; (ii) mitochondrial membrane potential (MMP); (iii) mitochondrial DNA (mtDNA) content and (iv) proteins involved in mitochondrial dynamics, mitofusin 1 (Mfn1) and dynamin related protein 1 (Dr

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Ma, Yu, Yujing Zhang, Yuanyuan Xiao, and Fang Xiao. "Increased Mitochondrial Fragmentation Mediated by Dynamin-Related Protein 1 Contributes to Hexavalent Chromium-Induced Mitochondrial Respiratory Chain Complex I-Dependent Cytotoxicity." Toxics 8, no. 3 (2020): 50. http://dx.doi.org/10.3390/toxics8030050.

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Hexavalent chromium (Cr(VI)) pollution is a severe public health problem in the world. Although it is believed that mitochondrial fragmentation is a common phenomenon in apoptosis, whether excessive fission is crucial for apoptosis remains controversial. We previously confirmed that Cr(VI) mainly targeted mitochondrial respiratory chain complex I (MRCC I) to induce reactive oxygen species (ROS)-mediated apoptosis, but the related mechanism was unclear. In this study, we found Cr(VI) targeted MRCC I to induce ROS accumulation and triggered mitochondria-related cytotoxicity. Cr(VI)-induced cytot

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Ma, Jun, and Fei Sun. "Expression, purification, crystallization and preliminary crystallographic study of the cytoplasmic domain of the mitochondrial dynamics protein MiD51." Acta Crystallographica Section F Structural Biology Communications 70, no. 5 (2014): 596–99. http://dx.doi.org/10.1107/s2053230x14006827.

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Mitochondria play central roles in many cellular and physiological processes. They are highly dynamic organelles and continually undergo fusion and fission. Mitochondrial dynamics protein 51 kDa (MiD51), an integral mitochondrial outer membrane protein, recruits dynamin-related protein 1 (Drp1; a mitochondrial fission protein) to mitochondria and facilitates Drp1-directed mitochondrial fission. In this study, the cytoplasmic domain of MiD51 was overexpressed inEscherichia coli, purified and crystallized. An X-ray diffraction data set was collected to a resolution of 3.1 Å and the crystal belon

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Zhang, Juan, Yu Zhang, Wenshuang Wu, et al. "Guanylate-binding protein 2 regulates Drp1-mediated mitochondrial fission to suppress breast cancer cell invasion." Cell Death & Disease 8, no. 10 (2017): e3151-e3151. http://dx.doi.org/10.1038/cddis.2017.559.

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Abstract Guanylate-binding protein 2 (GBP2) is a member of the large GTPase superfamily that is strongly induced by interferon-γ (IFN-γ). Although the biochemical characteristics of GBP2 have been reported in detail, its biological function has not been thoroughly elucidated to date. To the best of our knowledge, this study presents the first demonstration that GBP2 inhibits mitochondrial fission and cell metastasis in breast cancer cells both in vitro and in vivo. Our previous work demonstrated that dynamin-related protein 1 (Drp1)-dependent mitochondrial fission has a key role in breast canc

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Pryde, Kenneth R., Heather L. Smith, Kai-Yin Chau, and Anthony H. V. Schapira. "PINK1 disables the anti-fission machinery to segregate damaged mitochondria for mitophagy." Journal of Cell Biology 213, no. 2 (2016): 163–71. http://dx.doi.org/10.1083/jcb.201509003.

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Mitochondrial fission is essential for the degradation of damaged mitochondria. It is currently unknown how the dynamin-related protein 1 (DRP1)–associated fission machinery is selectively targeted to segregate damaged mitochondria. We show that PTEN-induced putative kinase (PINK1) serves as a pro-fission signal, independently of Parkin. Normally, the scaffold protein AKAP1 recruits protein kinase A (PKA) to the outer mitochondrial membrane to phospho-inhibit DRP1. We reveal that after damage, PINK1 triggers PKA displacement from A-kinase anchoring protein 1. By ejecting PKA, PINK1 ensures the

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Longo, Fabiana, Sara Benedetti, Alberto A. Zambon, et al. "Impaired turnover of hyperfused mitochondria in severe axonal neuropathy due to a novel DRP1 mutation." Human Molecular Genetics 29, no. 2 (2019): 177–88. http://dx.doi.org/10.1093/hmg/ddz211.

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Abstract Mitochondria undergo continuous cycles of fusion and fission in response to physiopathological stimuli. The key player in mitochondrial fission is dynamin-related protein 1 (DRP1), a cytosolic protein encoded by dynamin 1-like (DNM1L) gene, which relocalizes to the outer mitochondrial membrane, where it assembles, oligomerizes and drives mitochondrial division upon guanosine-5′-triphosphate (GTP) hydrolysis. Few DRP1 mutations have been described so far, with patients showing complex and variable phenotype ranging from early death to encephalopathy and/or optic atrophy. The disease is

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Tang, Jiayu, Zhiping Hu, Jieqiong Tan, Sonlin Yang, and Liuwang Zeng. "Parkin Protects against Oxygen-Glucose Deprivation/Reperfusion Insult by Promoting Drp1 Degradation." Oxidative Medicine and Cellular Longevity 2016 (2016): 1–10. http://dx.doi.org/10.1155/2016/8474303.

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Ischemic stroke results in severe brain damage and remains one of the leading causes of death and disability worldwide. Effective neuroprotective therapies are needed to reduce brain damage resulting from ischemic stroke. Mitochondria are crucial for cellular energy production and homeostasis. Modulation of mitochondrial function mediates neuroprotection against ischemic brain damage. Dynamin-related protein 1 (Drp1) and parkin play a key role in regulating mitochondrial dynamics. They are potential therapeutic targets for neuroprotection in ischemic stroke. Protective effects of parkin-Drp1 p

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Wasiak, Sylwia, Rodolfo Zunino, and Heidi M. McBride. "Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death." Journal of Cell Biology 177, no. 3 (2007): 439–50. http://dx.doi.org/10.1083/jcb.200610042.

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Dynamin-related protein 1 (DRP1) plays an important role in mitochondrial fission at steady state and during apoptosis. Using fluorescence recovery after photobleaching, we demonstrate that in healthy cells, yellow fluorescent protein (YFP)–DRP1 recycles between the cytoplasm and mitochondria with a half-time of 50 s. Strikingly, during apoptotic cell death, YFP-DRP1 undergoes a transition from rapid recycling to stable membrane association. The rapid cycling phase that characterizes the early stages of apoptosis is independent of Bax/Bak. However, after Bax recruitment to the mitochondrial me

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Froehlich, Theresa, Andreas Jenner, Claudia Cavarischia-Rega, et al. "Nanobodies as novel tools to monitor the mitochondrial fission factor Drp1." Life Science Alliance 7, no. 8 (2024): e202402608. http://dx.doi.org/10.26508/lsa.202402608.

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In cells, mitochondria undergo constant fusion and fission. An essential factor for fission is the mammalian dynamin-related protein 1 (Drp1). Dysregulation of Drp1 is associated with neurodegenerative diseases including Parkinson’s, cardiovascular diseases and cancer, making Drp1 a pivotal biomarker for monitoring mitochondrial status and potential pathophysiological conditions. Here, we developed nanobodies (Nbs) as versatile binding molecules for proteomics, advanced microscopy and live cell imaging of Drp1. To specifically enrich endogenous Drp1 with interacting proteins for proteomics, we

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Richter, Viviane, Catherine S. Palmer, Laura D. Osellame, et al. "Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission." Journal of Cell Biology 204, no. 4 (2014): 477–86. http://dx.doi.org/10.1083/jcb.201311014.

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Mitochondrial fission is important for organelle transport, inheritance, and turnover, and alterations in fission are seen in neurological disease. In mammals, mitochondrial fission is executed by dynamin-related protein 1 (Drp1), a cytosolic guanosine triphosphatase that polymerizes and constricts the organelle. Recruitment of Drp1 to mitochondria involves receptors including Mff, MiD49, and MiD51. MiD49/51 form foci at mitochondrial constriction sites and coassemble with Drp1 to drive fission. Here, we solved the crystal structure of the cytosolic domain of human MiD51, which adopts a nucleo

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Chandra, Partha K., Ibolya Rutkai, Hogyoung Kim, et al. "Latent HIV-Exosomes Induce Mitochondrial Hyperfusion Due to Loss of Phosphorylated Dynamin-Related Protein 1 in Brain Endothelium." Molecular Neurobiology 58, no. 6 (2021): 2974–89. http://dx.doi.org/10.1007/s12035-021-02319-8.

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AbstractDamage to the cerebral vascular endothelium is a critical initiating event in the development of HIV-1-associated neurocognitive disorders. To study the role of mitochondria in cerebral endothelial dysfunction, we investigated how exosomes, isolated from both cell lines with integrated provirus and HIV-1 infected primary cells (HIV-exosomes), accelerate the dysfunction of primary human brain microvascular endothelial cells (HBMVECs) by inducing mitochondrial hyperfusion, and reducing the expression of phosphorylated endothelial nitric oxide synthase (p-eNOS). The quantitative analysis

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Watanabe, T., M. S. Saotome, M. N. Nobuhara, et al. "Dynamin-Related Protein 1 (DRP1) manipulates myocardial insulin resistance through mitochondrial ROS production." European Heart Journal 34, suppl 1 (2013): 1756. http://dx.doi.org/10.1093/eurheartj/eht308.1756.

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Moore, Timothy M., Zhenqi Zhou, Amanda J. Lin, et al. "The Role Of Dynamin-related Protein 1 (drp1) In The Adaptations To Exercise." Medicine & Science in Sports & Exercise 50, no. 5S (2018): 114–15. http://dx.doi.org/10.1249/01.mss.0000535461.35442.02.

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Lee, Youngil, Hwa-Youn Lee, Rita A. Hanna, and Åsa B. Gustafsson. "Mitochondrial autophagy by Bnip3 involves Drp1-mediated mitochondrial fission and recruitment of Parkin in cardiac myocytes." American Journal of Physiology-Heart and Circulatory Physiology 301, no. 5 (2011): H1924—H1931. http://dx.doi.org/10.1152/ajpheart.00368.2011.

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The Bcl2/adenovirus E1B 19-kDa interacting protein 3 (Bnip3) is an atypical BH3-only protein that is associated with mitochondrial dysfunction and cell death. Bnip3 is also a potent inducer of mitochondrial autophagy, and in this study we have investigated the mechanisms by which Bnip3 induces autophagy in cardiac myocytes. We found that Bnip3 induced mitochondrial translocation of dynamin-related protein 1 (Drp1), a protein involved in mitochondrial fission in adult myocytes. Drp1-mediated mitochondrial fission correlated with increased autophagy, and inhibition of Drp1 reduced Bnip3-mediated

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Huang, Shiyuan, Xiaona Wang, Xinmei Wu, et al. "Yap regulates mitochondrial structural remodeling during myoblast differentiation." American Journal of Physiology-Cell Physiology 315, no. 4 (2018): C474—C484. http://dx.doi.org/10.1152/ajpcell.00112.2018.

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Yes-associated protein (Yap) is a core transcriptional coactivator in the downstream Hippo pathway that regulates cell proliferation and tissue growth. However, its role in the regulation of myoblast differentiation remains unclear. Regulation of mitochondrial networks by dynamin-related protein 1 (Drp1) and mitofusion 2 (Mfn2) is crucial for the activation of myoblast differentiation. In the present study, we investigated the interplay between the Hippo/Yap pathway and protein contents of Mfn2 and Drp1 during myoblast differentiation. The Hippo/Yap pathway was inactivated at the early stage o

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Gilkerson, Robert, Harpreet Kaur, Omar Carrillo, and Isaiah Ramos. "OMA1-Mediated Mitochondrial Dynamics Balance Organellar Homeostasis Upstream of Cellular Stress Responses." International Journal of Molecular Sciences 25, no. 8 (2024): 4566. http://dx.doi.org/10.3390/ijms25084566.

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In response to cellular metabolic and signaling cues, the mitochondrial network employs distinct sets of membrane-shaping factors to dynamically modulate organellar structures through a balance of fission and fusion. While these organellar dynamics mediate mitochondrial structure/function homeostasis, they also directly impact critical cell-wide signaling pathways such as apoptosis, autophagy, and the integrated stress response (ISR). Mitochondrial fission is driven by the recruitment of the cytosolic dynamin-related protein-1 (DRP1), while fusion is carried out by mitofusins 1 and 2 (in the o

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Yuan, Yanggang, Aiqing Zhang, Jia Qi, et al. "p53/Drp1-dependent mitochondrial fission mediates aldosterone-induced podocyte injury and mitochondrial dysfunction." American Journal of Physiology-Renal Physiology 314, no. 5 (2018): F798—F808. http://dx.doi.org/10.1152/ajprenal.00055.2017.

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Mitochondrial dysfunction is increasingly recognized as an important factor in glomerular diseases. Previous study has shown that mitochondrial fission contributed to mitochondrial dysfunction. However, the mechanism of mitochondrial fission on mitochondrial dysfunction in aldosterone-induced podocyte injury remains ambiguous. This study aimed to investigate the pathogenic effect of mitochondrial fission both in vivo and in vitro. In an animal model of aldosterone-induced nephropathy, inhibition of the mitochondrial fission protein dynamin-related protein 1 (Drp1) suppressed aldosterone-induce

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Nguyen, Nicholas, Meifang Yu, Vinit Reddy, et al. "Comparative Untargeted Metabolomic Profiling of Induced Mitochondrial Fusion in Pancreatic Cancer." Metabolites 11, no. 9 (2021): 627. http://dx.doi.org/10.3390/metabo11090627.

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Mitochondria are dynamic organelles that constantly alter their shape through the recruitment of specialized proteins, like mitofusin-2 (Mfn2) and dynamin-related protein 1 (Drp1). Mfn2 induces the fusion of nearby mitochondria, while Drp1 mediates mitochondrial fission. We previously found that the genetic or pharmacological activation of mitochondrial fusion was tumor suppressive against pancreatic ductal adenocarcinoma (PDAC) in several model systems. The mechanisms of how these different inducers of mitochondrial fusion reduce pancreatic cancer growth are still unknown. Here, we characteri

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Haun, Florian, Tomohiro Nakamura, and Stuart A. Lipton. "Dysfunctional Mitochondrial Dynamics in the Pathophysiology of Neurodegenerative Diseases." Journal of Cell Death 6 (January 2013): JCD.S10847. http://dx.doi.org/10.4137/jcd.s10847.

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Mitochondrial dysfunction occurs in neurodegenerative diseases, however molecular mechanisms underlying this process remain elusive. Emerging evidence suggests that nitrosative stress, mediated by reactive nitrogen species (RNS), may play a role in mitochondrial pathology. Here, we review findings that highlight the abnormal mitochondrial morphology observed in many neurodegenerative disorders including Alzheimer's, Parkinson's, and Huntington's diseases. One mechanism whereby RNS can affect mitochondrial function and thus neuronal survival occurs via protein S-nitrosylation, representing chem

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Kim, Boa, Ji-Seok Kim, Yisang Yoon, Mayra C. Santiago, Michael D. Brown, and Joon-Young Park. "Inhibition of Drp1-dependent mitochondrial division impairs myogenic differentiation." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 305, no. 8 (2013): R927—R938. http://dx.doi.org/10.1152/ajpregu.00502.2012.

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Mitochondria are dynamic organelles forming a tubular network that is continuously fusing and dividing to control their morphology and functions. Recent literature has shed new light on a potential link between the dynamic behavior of mitochondria and muscle development. In this study, we investigate the role of mitochondrial fission factor dynamin-related protein 1 (Drp1) in myogenic differentiation. We found that differentiation of C2C12 myoblasts induced by serum starvation was accompanied by a gradual increase in Drp1 protein expression (to ∼350% up to 3 days) and a fast reduction of Drp1

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Mohammad, Ghulam, and Renu A. Kowluru. "Mitochondrial Dynamics in the Metabolic Memory of Diabetic Retinopathy." Journal of Diabetes Research 2022 (March 31, 2022): 1–14. http://dx.doi.org/10.1155/2022/3555889.

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Mitochondria play a central role in the development of diabetic retinopathy and in the metabolic memory associated with its continued progression. Mitochondria have a regulated fusion fission process, which is essential for their homeostasis. One of the major fission proteins, dynamin-related protein 1 (Drp1), is recruited to the mitochondria by fission protein 1 (Fis1) to initiate fragmentation. Our aim is to investigate the role of Drp1 in the altered mitochondrial dynamics in the continued progression of diabetic retinopathy. Methods. Drp1 activation, mitochondrial transport, and Drp1-Fis1

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Rogers, Maximillian A., Joshua D. Hutcheson, Takehito Okui, et al. "Dynamin-related protein 1 inhibition reduces hepatic PCSK9 secretion." Cardiovascular Research, February 22, 2021. http://dx.doi.org/10.1093/cvr/cvab034.

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Abstract Aims Proteostasis maintains protein homeostasis and participates in regulating critical cardiometabolic disease risk factors including proprotein convertase subtilisin/kexin type 9 (PCSK9). Endoplasmic reticulum (ER) remodeling through release and incorporation of trafficking vesicles mediates protein secretion and degradation. We hypothesized that ER remodeling that drives mitochondrial fission participates in cardiometabolic proteostasis. Methods and results We used in vitro and in vivo hepatocyte inhibition of a protein involved in mitochondrial fission, dynamin-related protein 1 (

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Umezu, Ryuta, Jun-ichiro Koga, Tetsuya Matoba, et al. "Macrophage (Drp1) Dynamin-Related Protein 1 Accelerates Intimal Thickening After Vascular Injury." Arteriosclerosis, Thrombosis, and Vascular Biology 40, no. 7 (2020). http://dx.doi.org/10.1161/atvbaha.120.314383.

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Objective: Mitochondria consistently change their morphology in a process regulated by proteins, including Drp1 (dynamin-related protein 1), a protein promoting mitochondrial fission. Drp1 is involved in the mechanisms underlying various cardiovascular diseases, such as myocardial ischemia/reperfusion injury, heart failure, and pulmonary arterial hypertension. However, its role in macrophages, which promote various vascular diseases, is poorly understood. We therefore tested our hypothesis that macrophage Drp1 promotes vascular remodeling after injury. Method and Results: To explore the select

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