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Journal articles on the topic 'Autophagic lysosome reformation (ALR)'

Author: Grafiati

Published: 7 July 2024

Last updated: 31 July 2025

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1

Zhang, Lu, Yu Fang, Xuan Cheng та ін. "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-

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2

Chen, Yang, and Li Yu. "Autophagic lysosome reformation." Experimental Cell Research 319, no. 2 (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 (2017): 358–61. http://dx.doi.org/10.1111/tra.12484.

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4

Toifl, Stefanie, Sebastian Didusch, Karin Ehrenreiter, Enrico Desideri, Coralie Dorard, and Manuela Baccarini. "RAF1 kinase contributes to autophagic lysosome reformation." Cell Reports 44, no. 4 (2025): 115490. https://doi.org/10.1016/j.celrep.2025.115490.

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5

Gan, Qiwen, Xin Wang, Qian Zhang, 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 (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 lysoso

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6

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

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7

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

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8

Rong, Y., C. K. McPhee, S. Deng, et al. "Spinster is required for autophagic lysosome reformation and mTOR reactivation following starvation." Proceedings of the National Academy of Sciences 108, no. 19 (2011): 7826–31. http://dx.doi.org/10.1073/pnas.1013800108.

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9

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 (2016): 3432–45. http://dx.doi.org/10.1093/hmg/ddw185.

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10

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

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11

Mai, Xinyi, Yang Wang, Xi Wang, et al. "BPS2025 - Understanding autophagic lysosome reformation: Structural insights into the AP5:SPG11-SPG15 complex." Biophysical Journal 124, no. 3 (2025): 227a. https://doi.org/10.1016/j.bpj.2024.11.1247.

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12

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 (2023): 957–58. http://dx.doi.org/10.4103/1673-5374.385298.

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13

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 (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

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14

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 (2021): 1287–89. http://dx.doi.org/10.1080/15548627.2021.1916195.

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15

Vantaggiato, Chiara, Genny Orso, Giulia Guarato, 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

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16

Wang, Weihua, Chu Han, Shengjie Xie, et al. "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 lysoso

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17

Nanayakkara, Randini, Rajendra Gurung, Samuel J. Rodgers, et al. "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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18

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

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19

Serra-Vinardell, Jenny, Maxwell B. Sandler, Raffaella De Pace, 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 (2023). http://dx.doi.org/10.1007/s00018-023-04724-9.

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20

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 (2018). http://dx.doi.org/10.1002/cpcb.44.

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21

Cantarero, Lara, Elena Juárez-Escoto, Azahara Civera-Tregón, et al. "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 trafficki

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22

Kumar, Gaurav, Prateek Chawla, Neha Dhiman, et al. "RUFY3 links Arl8b and JIP4-Dynein complex to regulate lysosome size and positioning." Nature Communications 13, no. 1 (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 endos

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23

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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24

Bhattacharya, Anshu, Rukmini Mukherjee, Santosh Kumar Kuncha, et al. "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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25

Calcagni’, Alessia, Leopoldo Staiano, Nicolina Zampelli, 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 (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 lysosom

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26

Khundadze, Mukhran, Federico Ribaudo, Adeela Hussain, 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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27

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 (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 expl

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28

Singh, Amruta, Kewal Kumar Mahapatra, Prakash Priyadarshi Praharaj, et al. "Prolonged glutamine starvation reactivates mTOR to inhibit autophagy and initiate autophagic lysosome reformation to maintain cell viability." International Journal of Biochemistry & Cell Biology, November 2024, 106694. http://dx.doi.org/10.1016/j.biocel.2024.106694.

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29

"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 (2011): 11297. http://dx.doi.org/10.1073/pnas.1108410108.

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30

Daly, James L., Chris M. Danson, Philip A. Lewis, et al. "Multi-omic approach characterises the neuroprotective role of retromer in regulating lysosomal health." Nature Communications 14, no. 1 (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 with

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31

Wang, Feng, Yuxi Dai, Xufeng Zhu, et al. "Saturated very long chain fatty acid configures glycosphingolipid for lysosome homeostasis in long-lived C. elegans." Nature Communications 12, no. 1 (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 lifesp

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