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Статті в журналах з теми "Autophagic lysosome reformation (ALR)"

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Автор: Grafiati

Опубліковано: 7 липня 2024

Оновлено: 7 липня 2024

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1

Zhang, Lu, Yu Fang, Xuan Cheng, Yajun Lian, Hongliang Xu, Zhaoshu Zeng та Hongcan Zhu. "TRPML1 Participates in the Progression of Alzheimer’s Disease by Regulating the PPARγ/AMPK/Mtor Signalling Pathway". Cellular Physiology and Biochemistry 43, № 6 (2017): 2446–56. http://dx.doi.org/10.1159/000484449.

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Background: TRPML1 is reported to be involved in the pathogenesis of Alzheimer’s disease (AD) by regulating autophagy; however, the underlying mechanism is not completely clear. Methods: We developed an APP/PS1 transgenic animal model that presents with AD. TRPML1 was also overexpressed in these mice. Protein expression levels were determined by Western blot. Morris water maze (MWM) and recognition tasks were performed to characterize cognitive ability. TUNEL assays were analysed for the detection of neuronal apoptosis. Primary neurons were isolated and treated with the vehicle, Aβ1-42 or Aβ1-42 + mTOR activator, as well as infected with the recombinant adenovirus TRPML1 overexpression vector in vitro. Cell viability was measured by the MTS assay, and lysosomal Ca2+ was also measured. Results: In the APP/PS1 transgenic mice, TRPML1 was downregulated, the PPARγ/AMPK signalling pathway was activated, the mTOR/S6K signalling pathway was suppressed, and autophagic lysosome reformation (ALR)-related proteins were upregulated. TRPML1 overexpression or treatment with PPARγ and AMPK inhibitors or an mTOR activator reduced the expression levels of ALR-related proteins, rescued the memory and recognition impairments and attenuated neuronal apoptosis in mice with the APP/PS1 transgenes. In vitro experiments showed that TRPML1 overexpression or treatment with the mTOR activator propranolol attenuated the Aβ1-42-suppressed cell viability and the Aβ1-42-decreased lysosomal [Ca2+] ion concentration in primary neurons. TRPML1 overexpression or treatment with the mTOR activator propranolol also attenuated the Aβ1-42-inhibited mTOR/S6K signalling pathway and the Aβ1-42-induced ALR-related protein expression levels. Conclusion: TRPML1 is involved in the pathogenesis of AD by regulating autophagy at least in part through the PPARγ/AMPK/mTOR signallingpathway.

2

Chen, Yang, and Li Yu. "Autophagic lysosome reformation." Experimental Cell Research 319, no. 2 (January 2013): 142–46. http://dx.doi.org/10.1016/j.yexcr.2012.09.004.

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3

Chen, Yang, and Li Yu. "Recent progress in autophagic lysosome reformation." Traffic 18, no. 6 (May 5, 2017): 358–61. http://dx.doi.org/10.1111/tra.12484.

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4

Gan, Qiwen, Xin Wang, Qian Zhang, Qiuyuan Yin, Youli Jian, Yubing Liu, Nan Xuan, et al. "The amino acid transporter SLC-36.1 cooperates with PtdIns3P 5-kinase to control phagocytic lysosome reformation." Journal of Cell Biology 218, no. 8 (June 24, 2019): 2619–37. http://dx.doi.org/10.1083/jcb.201901074.

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Phagocytic removal of apoptotic cells involves formation, maturation, and digestion of cell corpse–containing phagosomes. The retrieval of lysosomal components following phagolysosomal digestion of cell corpses remains poorly understood. Here we reveal that the amino acid transporter SLC-36.1 is essential for lysosome reformation during cell corpse clearance in Caenorhabditis elegans embryos. Loss of slc-36.1 leads to formation of phagolysosomal vacuoles arising from cell corpse–containing phagosomes. In the absence of slc-36.1, phagosome maturation is not affected, but the retrieval of lysosomal components is inhibited. Moreover, loss of PPK-3, the C. elegans homologue of the PtdIns3P 5-kinase PIKfyve, similarly causes accumulation of phagolysosomal vacuoles that are defective in phagocytic lysosome reformation. SLC-36.1 and PPK-3 function in the same genetic pathway, and they directly interact with one another. In addition, loss of slc-36.1 and ppk-3 causes strong defects in autophagic lysosome reformation in adult animals. Our findings thus suggest that the PPK-3–SLC-36.1 axis plays a central role in both phagocytic and autophagic lysosome formation.

5

Rong, Yueguang, Mei Liu, Liang Ma, Wanqing Du, Hanshuo Zhang, Yuan Tian, Zhen Cao, et al. "Clathrin and phosphatidylinositol-4,5-bisphosphate regulate autophagic lysosome reformation." Nature Cell Biology 14, no. 9 (August 12, 2012): 924–34. http://dx.doi.org/10.1038/ncb2557.

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6

Chang, Jaerak, Seongju Lee, and Craig Blackstone. "Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation." Journal of Clinical Investigation 124, no. 12 (November 3, 2014): 5249–62. http://dx.doi.org/10.1172/jci77598.

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7

Rong, Y., C. K. McPhee, S. Deng, L. Huang, L. Chen, M. Liu, K. Tracy, E. H. Baehrecke, L. Yu, and M. J. Lenardo. "Spinster is required for autophagic lysosome reformation and mTOR reactivation following starvation." Proceedings of the National Academy of Sciences 108, no. 19 (April 25, 2011): 7826–31. http://dx.doi.org/10.1073/pnas.1013800108.

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8

Magalhaes, Joana, Matthew E. Gegg, Anna Migdalska-Richards, Mary K. Doherty, Phillip D. Whitfield, and Anthony H. V. Schapira. "Autophagic lysosome reformation dysfunction in glucocerebrosidase deficient cells: relevance to Parkinson disease." Human Molecular Genetics 25, no. 16 (July 4, 2016): 3432–45. http://dx.doi.org/10.1093/hmg/ddw185.

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9

Liu, Xu, and Daniel J. Klionsky. "Regulation of autophagic lysosome reformation by kinesin 1, clathrin and phosphatidylinositol-4,5-bisphosphate." Autophagy 14, no. 1 (December 21, 2017): 1–2. http://dx.doi.org/10.1080/15548627.2017.1386821.

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10

Sharma, Prashant, Jenny Serra-Vinardell, Wendy J. Introne, and May Christine V. Malicdan. "Role of lysosomal trafficking regulator in autophagic lysosome reformation in neurons: a disease perspective." Neural Regeneration Research 19, no. 5 (September 22, 2023): 957–58. http://dx.doi.org/10.4103/1673-5374.385298.

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11

Sánchez-Porras, Valentina, Johana Maria Guevara-Morales, and Olga Yaneth Echeverri-Peña. "From Acid Alpha-Glucosidase Deficiency to Autophagy: Understanding the Bases of POMPE Disease." International Journal of Molecular Sciences 24, no. 15 (August 5, 2023): 12481. http://dx.doi.org/10.3390/ijms241512481.

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Pompe disease (PD) is caused by mutations in the GAA gene, which encodes the lysosomal enzyme acid alpha-glucosidase, causing lysosomal glycogen accumulation, mainly in muscular tissue. Autophagic buildup is considered the main factor affecting skeletal muscle, although other processes are also involved. Uncovering how these mechanisms are interconnected could be an approximation to address long-lasting concerns, like the differential skeletal and cardiac involvement in each clinical phenotype. In this sense, a network reconstruction based on a comprehensive literature review of evidence found in PD enriched with the STRING database and other scientific articles is presented. The role of autophagic lysosome reformation, PGC-1α, MCOLN1, calcineurin, and Keap1 as intermediates between the events involved in the pathologic cascade is discussed and contextualized within their relationship with mTORC1/AMPK. The intermediates and mechanisms found open the possibility of new hypotheses and questions that can be addressed in future experimental studies of PD.

12

Eramo, Matthew J., Rajendra Gurung, Christina A. Mitchell, and Meagan J. McGrath. "Bidirectional interconversion between PtdIns4P and PtdIns(4,5)P2 is required for autophagic lysosome reformation and protection from skeletal muscle disease." Autophagy 17, no. 5 (April 20, 2021): 1287–89. http://dx.doi.org/10.1080/15548627.2021.1916195.

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13

Vantaggiato, Chiara, Genny Orso, Giulia Guarato, Francesca Brivio, Barbara Napoli, Elena Panzeri, Simona Masotti, et al. "Rescue of lysosomal function as therapeutic strategy for SPG15 hereditary spastic paraplegia." Brain, August 27, 2022. http://dx.doi.org/10.1093/brain/awac308.

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Abstract SPG15 is a hereditary spastic paraplegia (HSP) subtype caused by mutations in Spastizin, a protein encoded by the ZFYVE26 gene. Spastizin is involved in autophagosome maturation and autophagic lysosome reformation (ALR) and SPG15-related mutations lead to ALR defects with lysosome enlargement, free lysosomes depletion and autophagosome accumulation. Symptomatic and rehabilitative treatments are the only therapy currently available for patients. Here, we targeted autophagy and lysosomes in SPG15 patient-derived cells by using a library of autophagy-modulating compounds. We identified a rose of compounds, affecting intracellular calcium levels, the calcium-calpain pathway, or lysosomal functions, that reduced autophagosome accumulation. The six most effective compounds were tested in vivo in a new SPG15 loss of function Drosophila model that mimicked the reported SPG15 phenotype, with autophagosome accumulation, enlarged lysosomes, reduced free lysosomes, ALR defects and locomotor deficit. These compounds, namely verapamil, Bay K8644, 2’,5’-dideoxyadenosine, trehalose, Small Molecule Enhancer of Rapamycin 28 (SMER28) and trifluoperazine, improved lysosome biogenesis and function in vivo, demonstrating that lysosomes are a key pharmacological target to rescue SPG15 phenotype. Among the others, the small molecule enhancer of autophagy SMER28 was the most effective, rescuing both ALR defects and locomotor deficit, and could be considered as a potential therapeutic compound for this HSP subtype.

14

Wang, Weihua, Chu Han, Shengjie Xie, Zisong Cong, Zixuan Yang, Yuxin Feng, Limin Xiang, and Heng Song. "A high‐contrast autolysosome probe for detecting interaction between autophagosomes and autolysosomes in mitophagy." Chinese Journal of Chemistry, December 19, 2023. http://dx.doi.org/10.1002/cjoc.202300639.

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Comprehensive SummaryAutophagy is a multi‐step cell metabolism process in which cells remove damaged and unwanted materials. During autophagy, autophagosomes fuse with lysosomes to form autophagosomes. Autophagosomal membrane components are recycled from autolysosomes through the autophagosomal components recycling (ACR), while lysosomal components circulate on the autolysosomal surface through the autophagic lysosome reformation (ALR) process. Autolysosomes contain components from autophagosomes and lysosomes. However, whether there is a fusion between autolysosome and autophagosome or lysosome at the organelle level remains unknown. In this study, a pH and viscosity dual‐controlled mitochondria‐targeting fluorescent probe Mito‐Q was designed based on an asymmetric norcyanine to achieve the high‐contrast imaging of mitochondria‐containing autolysosomes. Mito‐Q not only effectively detected mitochondrial viscosity changes and mitophagy with high sensitivity, but more importantly, the fusion of mitochondria‐containing autolysosomes and autophagosomes (FMAA) was observed during autophagy by the real‐time confocal imaging of HeLa cells.This article is protected by copyright. All rights reserved.

15

Nanayakkara, Randini, Rajendra Gurung, Samuel J. Rodgers, Matthew J. Eramo, Georg Ramm, Christina A. Mitchell, and Meagan J. McGrath. "Autophagic lysosome reformation in health and disease." Autophagy, November 21, 2022, 1–18. http://dx.doi.org/10.1080/15548627.2022.2128019.

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16

Serra-Vinardell, Jenny, Maxwell B. Sandler, Raffaella De Pace, Javier Manzella-Lapeira, Antony Cougnoux, Keyvan Keyvanfar, Wendy J. Introne, et al. "LYST deficiency impairs autophagic lysosome reformation in neurons and alters lysosome number and size." Cellular and Molecular Life Sciences 80, no. 2 (January 28, 2023). http://dx.doi.org/10.1007/s00018-023-04695-x.

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17

Serra-Vinardell, Jenny, Maxwell B. Sandler, Raffaella De Pace, Javier Manzella-Lapeira, Antony Cougnoux, Keyvan Keyvanfar, Wendy J. Introne, et al. "Correction: LYST deficiency impairs autophagic lysosome reformation in neurons and alters lysosome number and size." Cellular and Molecular Life Sciences 80, no. 3 (March 2023). http://dx.doi.org/10.1007/s00018-023-04724-9.

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18

Chen, Yang, Qian Peter Su, Yujie Sun, and Li Yu. "Visualizing Autophagic Lysosome Reformation in Cells Using In Vitro Reconstitution Systems." Current Protocols in Cell Biology 78, no. 1 (March 2018). http://dx.doi.org/10.1002/cpcb.44.

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19

Cantarero, Lara, Elena Juárez-Escoto, Azahara Civera-Tregón, María Rodríguez-Sanz, Mónica Roldán, Raúl Benítez, Janet Hoenicka, and Francesc Palau. "Mitochondria–lysosome membrane contacts are defective in GDAP1-related Charcot–Marie–Tooth disease." Human Molecular Genetics, November 6, 2020. http://dx.doi.org/10.1093/hmg/ddaa243.

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Abstract Mutations in the GDAP1 gene cause Charcot–Marie–Tooth (CMT) neuropathy. GDAP1 is an atypical glutathione S-transferase (GST) of the outer mitochondrial membrane and the mitochondrial membrane contacts with the endoplasmic reticulum (MAMs). Here, we investigate the role of this GST in the autophagic flux and the membrane contact sites (MCSs) between mitochondria and lysosomes in the cellular pathophysiology of GDAP1 deficiency. We demonstrate that GDAP1 participates in basal autophagy and that its depletion affects LC3 and PI3P biology in autophagosome biogenesis and membrane trafficking from MAMs. GDAP1 also contributes to the maturation of lysosome by interacting with PYKfyve kinase, a pH-dependent master lysosomal regulator. GDAP1 deficiency causes giant lysosomes with hydrolytic activity, a delay in the autophagic lysosome reformation, and TFEB activation. Notably, we found that GDAP1 interacts with LAMP-1, which supports that GDAP1–LAMP-1 is a new tethering pair of mitochondria and lysosome membrane contacts. We observed mitochondria–lysosome MCSs in soma and axons of cultured mouse embryonic motor neurons and human neuroblastoma cells. GDAP1 deficiency reduces the MCSs between these organelles, causes mitochondrial network abnormalities, and decreases levels of cellular glutathione (GSH). The supply of GSH-MEE suffices to rescue the lysosome membranes and the defects of the mitochondrial network, but not the interorganelle MCSs nor early autophagic events. Overall, we show that GDAP1 enables the proper function of mitochondrial MCSs in both degradative and nondegradative pathways, which could explain primary insults in GDAP1-related CMT pathophysiology, and highlights new redox-sensitive targets in axonopathies where mitochondria and lysosomes are involved.

20

Swords, Sierra B., Nuo Jia, Anne Norris, Jil Modi, Qian Cai, and Barth D. Grant. "A conserved requirement for RME-8/DNAJC13 in neuronal autophagic lysosome reformation." Autophagy, November 9, 2023, 1–17. http://dx.doi.org/10.1080/15548627.2023.2269028.

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21

Kumar, Gaurav, Prateek Chawla, Neha Dhiman, Sanya Chadha, Sheetal Sharma, Kanupriya Sethi, Mahak Sharma, and Amit Tuli. "RUFY3 links Arl8b and JIP4-Dynein complex to regulate lysosome size and positioning." Nature Communications 13, no. 1 (March 21, 2022). http://dx.doi.org/10.1038/s41467-022-29077-y.

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AbstractThe bidirectional movement of lysosomes on microtubule tracks regulates their whole-cell spatial arrangement. Arl8b, a small GTP-binding (G) protein, promotes lysosome anterograde trafficking mediated by kinesin-1. Herein, we report an Arl8b effector, RUFY3, which regulates the retrograde transport of lysosomes. We show that RUFY3 interacts with the JIP4-dynein-dynactin complex and facilitates Arl8b association with the retrograde motor complex. Accordingly, RUFY3 knockdown disrupts the positioning of Arl8b-positive endosomes and reduces Arl8b colocalization with Rab7-marked late endosomal compartments. Moreover, we find that RUFY3 regulates nutrient-dependent lysosome distribution, although autophagosome-lysosome fusion and autophagic cargo degradation are not impaired upon RUFY3 depletion. Interestingly, lysosome size is significantly reduced in RUFY3 depleted cells, which could be rescued by inhibition of the lysosome reformation regulatory factor PIKFYVE. These findings suggest a model in which the perinuclear cloud arrangement of lysosomes regulates both the positioning and size of these proteolytic compartments.

22

Bhattacharya, Anshu, Rukmini Mukherjee, Santosh Kumar Kuncha, Melinda Elaine Brunstein, Rajeshwari Rathore, Stephan Junek, Christian Münch, and Ivan Dikic. "A lysosome membrane regeneration pathway depends on TBC1D15 and autophagic lysosomal reformation proteins." Nature Cell Biology, April 6, 2023. http://dx.doi.org/10.1038/s41556-023-01125-9.

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23

Calcagni’, Alessia, Leopoldo Staiano, Nicolina Zampelli, Nadia Minopoli, Niculin J. Herz, Giuseppe Di Tullio, Tuong Huynh, et al. "Loss of the batten disease protein CLN3 leads to mis-trafficking of M6PR and defective autophagic-lysosomal reformation." Nature Communications 14, no. 1 (July 3, 2023). http://dx.doi.org/10.1038/s41467-023-39643-7.

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AbstractBatten disease, one of the most devastating types of neurodegenerative lysosomal storage disorders, is caused by mutations in CLN3. Here, we show that CLN3 is a vesicular trafficking hub connecting the Golgi and lysosome compartments. Proteomic analysis reveals that CLN3 interacts with several endo-lysosomal trafficking proteins, including the cation-independent mannose 6 phosphate receptor (CI-M6PR), which coordinates the targeting of lysosomal enzymes to lysosomes. CLN3 depletion results in mis-trafficking of CI-M6PR, mis-sorting of lysosomal enzymes, and defective autophagic lysosomal reformation. Conversely, CLN3 overexpression promotes the formation of multiple lysosomal tubules, which are autophagy and CI-M6PR-dependent, generating newly formed proto-lysosomes. Together, our findings reveal that CLN3 functions as a link between the M6P-dependent trafficking of lysosomal enzymes and lysosomal reformation pathway, explaining the global impairment of lysosomal function in Batten disease.

24

Khundadze, Mukhran, Federico Ribaudo, Adeela Hussain, Henry Stahlberg, Nahal Brocke-Ahmadinejad, Patricia Franzka, Rita-Eva Varga, et al. "Mouse models for hereditary spastic paraplegia uncover a role of PI4K2A in autophagic lysosome reformation." Autophagy, March 9, 2021, 1–17. http://dx.doi.org/10.1080/15548627.2021.1891848.

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25

Hirst, Jennifer, Geoffrey G. Hesketh, Anne-Claude Gingras, and Margaret S. Robinson. "Rag GTPases and phosphatidylinositol 3-phosphate mediate recruitment of the AP-5/SPG11/SPG15 complex." Journal of Cell Biology 220, no. 2 (January 19, 2021). http://dx.doi.org/10.1083/jcb.202002075.

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Adaptor protein complex 5 (AP-5) and its partners, SPG11 and SPG15, are recruited onto late endosomes and lysosomes. Here we show that recruitment of AP-5/SPG11/SPG15 is enhanced in starved cells and occurs by coincidence detection, requiring both phosphatidylinositol 3-phosphate (PI3P) and Rag GTPases. PI3P binding is via the SPG15 FYVE domain, which, on its own, localizes to early endosomes. GDP-locked RagC promotes recruitment of AP-5/SPG11/SPG15, while GTP-locked RagA prevents its recruitment. Our results uncover an interplay between AP-5/SPG11/SPG15 and the mTORC1 pathway and help to explain the phenotype of AP-5/SPG11/SPG15 deficiency in patients, including the defect in autophagic lysosome reformation.

26

"Correction for Rong et al., Spinster is required for autophagic lysosome reformation and mTOR reactivation following starvation." Proceedings of the National Academy of Sciences 108, no. 27 (June 14, 2011): 11297. http://dx.doi.org/10.1073/pnas.1108410108.

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27

Wang, Feng, Yuxi Dai, Xufeng Zhu, Qilong Chen, Huanhu Zhu, Ben Zhou, Haiqing Tang, and Shanshan Pang. "Saturated very long chain fatty acid configures glycosphingolipid for lysosome homeostasis in long-lived C. elegans." Nature Communications 12, no. 1 (August 20, 2021). http://dx.doi.org/10.1038/s41467-021-25398-6.

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AbstractThe contents of numerous membrane lipids change upon ageing. However, it is unknown whether and how any of these changes are causally linked to lifespan regulation. Acyl chains contribute to the functional specificity of membrane lipids. In this study, working with C. elegans, we identified an acyl chain-specific sphingolipid, C22 glucosylceramide, as a longevity metabolite. Germline deficiency, a conserved lifespan-extending paradigm, induces somatic expression of the fatty acid elongase ELO-3, and behenic acid (22:0) generated by ELO-3 is incorporated into glucosylceramide for lifespan regulation. Mechanistically, C22 glucosylceramide is required for the membrane localization of clathrin, a protein that regulates membrane budding. The reduction in C22 glucosylceramide impairs the clathrin-dependent autophagic lysosome reformation, which subsequently leads to TOR activation and longevity suppression. These findings reveal a mechanistic link between membrane lipids and ageing and suggest a model of lifespan regulation by fatty acid-mediated membrane configuration.

28

Daly, James L., Chris M. Danson, Philip A. Lewis, Lu Zhao, Sara Riccardo, Lucio Di Filippo, Davide Cacchiarelli, et al. "Multi-omic approach characterises the neuroprotective role of retromer in regulating lysosomal health." Nature Communications 14, no. 1 (May 29, 2023). http://dx.doi.org/10.1038/s41467-023-38719-8.

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AbstractRetromer controls cellular homeostasis through regulating integral membrane protein sorting and transport and by controlling maturation of the endo-lysosomal network. Retromer dysfunction, which is linked to neurodegenerative disorders including Parkinson’s and Alzheimer’s diseases, manifests in complex cellular phenotypes, though the precise nature of this dysfunction, and its relation to neurodegeneration, remain unclear. Here, we perform an integrated multi-omics approach to provide precise insight into the impact of Retromer dysfunction on endo-lysosomal health and homeostasis within a human neuroglioma cell model. We quantify widespread changes to the lysosomal proteome, indicative of broad lysosomal dysfunction and inefficient autophagic lysosome reformation, coupled with a reconfigured cell surface proteome and secretome reflective of increased lysosomal exocytosis. Through this global proteomic approach and parallel transcriptomic analysis, we provide a holistic view of Retromer function in regulating lysosomal homeostasis and emphasise its role in neuroprotection.