Cited by 212Autophagy in Disease and TherapyMicrotubule and mitosis dynamicsCalcium signaling and nucleotide metabolism

The DOI matches its Crossref record; 110 of the 110 references it cites were found in a registry or an index.

Autophagy and microtubules - new story, old players

Mackeh, Rafah, Perdiz, Daniel, Lorin, Séverine, Codogno, Patrice, Poüs, Christian·2013·Journal of Cell Science

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Abstract

Summary: Both at a basal level and after induction (especially in response to nutrient starvation), the function of autophagy is to allow cells to degrade and recycle damaged organelles, proteins and other biological constituents. Here, we focus on the role microtubules have in autophagosome formation, autophagosome transport across the cytoplasm and in the formation of autolysosomes. Recent insights into the exact relationship between autophagy and microtubules now point to the importance of microtubule dynamics, tubulin post-translational modifications and microtubule motors in the autophagy process. Such factors regulate signaling pathways that converge to stimulate autophagosome formation. They also orchestrate the movements of pre-autophagosomal structures and autophagosomes or more globally organize and localize immature and mature autophagosomes and lysosomes. Most of the factors that now appear to link microtubules to autophagosome formation or to autophagosome dynamics and fate were identified initially without the notion that sequestration, recruitment and/or interaction with microtubules contribute to their function. Spatial and temporal coordination of many stages in the life of autophagosomes thus underlines the integrative role of microtubules and progressively reveals hidden parts of the autophagy machinery.

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Crossref · 10.1242/jcs.115626

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RETRACTED ARTICLE: The microtubule depolymerizing agent naphthazarin induces both apoptosis and autophagy in A549 lung cancer cells
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Background
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Background
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Background
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Background
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Background
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“To test this, we induced CNGs in a nocodazole-independent manner due to the fact that several studies demonstrated an essential role of microtubules in autophagosome formation (Mackeh et al., 2013) and used the siRNA specific to FXR1 which was previously shown to induce CNGs (Agote-Aran et al.”
Method
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Background
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“platform for intracellular transport, are involved in autophagosome formation and motility (15).”
Background
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Background
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“Although it is generally believed that basal autophagosome formation does not involve MT, stress-induced autophagosome formation requires proper MT function [48].”
Background
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Lombardo, T., Folgar, M. L. G., Salaverry, L. S., Rey-Roldán, E. B., Álvarez, É., Carreras, M. C., Kornblihtt, L. I., & Blanco, G. A. C. (2017) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.12945 · Cited by 7
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Wang, Y., Zheng, X., & Liu, Y. (2016) · Plant Signaling & Behavior · doi:10.1080/15592324.2016.1201626 · Cited by 3
Targeting Mitophagy in Combined Therapies of Haematological Malignancies
Kornblihtt, L. I., Carreras, M. C., & Blanco, G. A. C. (2016) · InTech eBooks · doi:10.5772/63306 · Cited by 4
“The transport of mitophagosomes and autophagosomes along the microtubule is required for fusion with lysosomes [36].”
Background
Repurposing Terfenadine as a Novel Antigiardial Compound
Suárez-Rico, D. O., Munguía-Huizar, F. J., Cortés-Zárate, R., Hernández‐Hernández, J. M., González‐Pozos, S., Pérez-Rangel, A., & Castillo‐Romero, A. (2023) · Pharmaceuticals · doi:10.3390/ph16091332 · Cited by 3
Does mTORC1 inhibit autophagy at dual stages?
Santhaseela, A. R., & Jayavelu, T. (2020) · Bioessays · doi:10.1002/bies.202000187 · Cited by 3
“[76] Considering the perinuclear localization of Rheb,[9,78,79] lysosomal fusion with autophagosome in the perinuclear region,[76] and the activation of mTORC1 on lysosomes promoting their movement from perinuclear to peripheral region,[68] a potential connection betweenmTORC1activation and lysosomal positioning may e…”
BackgroundInfluential
Microtubule-destabilizing agents enhance STING-mediated innate immune response via biased mechanism in human monocyte cells
Lim, S., Jung, H. R., Lee, H., Chu, Y., Kim, H., Kim, E., & Lee, S. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115883 · Cited by 3
A Transgenic Mouse Model of Eccentric Left Ventricular Hypertrophy With Preserved Ejection Fraction Exhibits Alterations in the Autophagy-Lysosomal Pathway
Wenzel, K., Krämer, E., Geertz, B., Carrier, L., Felix, S. B., Könemann, S., & Schlossarek, S. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.614878 · Cited by 3
“…flux and dysregulated expression of ALP key marker have been observed in a wide range of cardiac diseases such as desmin-related cardiomyopathy (Maloyan et al., 2010; Pattison et al., 2011; Bhuiyan et al., 2013), dilated cardiomyopathy (Choi et al., 2012; Ramos et al., 2012) and hypertrophic…”
Background
Microtubule inhibitors identified through nonbiased screening enhance DNA transfection efficiency by delaying p62‐dependent ubiquitin recruitment
Tsuchiya, M., Ogawa, H., Watanabe, K., Koujin, T., Mori, C., Nunomura, K., Lin, B., Tani, A., Hiraoka, Y., & Haraguchi, T. (2021) · Genes to Cells · doi:10.1111/gtc.12881 · Cited by 3
Cytoskeletal Proteins
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Microgravity Induces Interplay Between Atg8, Tua and Tub Gene Expression in Arabidopsis ThalianaPreprint
Shadrina, R., Yemets, A. I., Plokhovska, S., & Blume, Y. B. (2022) · Research Square · doi:10.21203/rs.3.rs-2119853/v1 · Cited by 3
FGF13 Deficiency Ameliorates Paclitaxel‐Induced Neuropathic Pain by Inhibiting VASH1‐Mediated Microtubule Detyrosination to Promote Mitophagy
Dong, Y., Wang, Y., Lv, S., Dong, Z., Zhi, K., Guo, X., Li, X., Yu, R., Zhang, Y. J., Cheng, S., et al. (2026) · Advanced Science · doi:10.1002/advs.202520995 · Cited by 2
The Drosophila Nesprin-1 homolog MSP300 is required for muscle autophagy and proteostasis
van der Graaf, K., Srivastav, S., Nishad, R., Stern, M., & McNew, J. A. (2024) · Journal of Cell Science · doi:10.1242/jcs.262096 · Cited by 2
Citrinin disrupts microtubule assembly in cardiac cells: Impact on mitochondrial organization and function
Tsai, J.-F., Yu, F., & Liu, B.-H. (2024) · Chemosphere · doi:10.1016/j.chemosphere.2024.143352 · Cited by 2
Unleash the dogs of death: metacaspase 5, microtubules, and hypersensitive response
Zhu, X., Zhang, K., Gong, P., Riemann, M., & Nick, P. (2025) · Plant Cell Reports · doi:10.1007/s00299-025-03567-x · Cited by 2
“The link between microtubules and autolysis might be evolutionarily ancient since it is well-known from animal cells (for review, see Mackeh et al .”
Molecular Machines Involved in Pexophagy
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Microtubule-Targeting Agents Induce ROS-Mediated Apoptosis in Cancer
Das, A. K., Paul, S., Chakrabarty, S., Dasgupta, M., & Chakrabarti, G. (2022) · Springer eBooks · doi:10.1007/978-981-15-9411-3_46 · Cited by 2
Truncated tau disrupts autophagy and lysosomal biogenesisPreprint
Dakkak, D., Pollack, S. J., Guo, T., Chennell, G., Gómez‐Suaga, P., Noble, W. J., & Hanger, D. P. (2022) · Research Square · doi:10.21203/rs.3.rs-1522321/v1 · Cited by 2
LRBA balances antigen presentation and T-cell responses via autophagy by binding to PIK3R4 and FYCO1Preprint
Sindram, E., Deau, M., Ligeon, L.-A., Sánchez‐Martín, P., Nestel, S., Jung, S., Ruf, S., Mishra, P., Proietti, M., Günther, S., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.17.512524 · Cited by 2
“FYCO1 is a multidomain adaptor protein that mediates microtubule plus-end-directed autophagosome transport by simultaneously interacting with kinesin motor proteins and autophagosomal proteins such as Rab7, LC3 and PI(3)P (14, 15, 31) .”
Background
Autophagy-related myosins: Critical roles and potential therapeutic effects in malignancies
Xiong, J., Wen, X., Chen, M., Liu, F., & Zhou, J. (2025) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2025.189375 · Cited by 1
The FSIP Family: Roles in Health and Cancer
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“…in promoting cell proliferation, FSIP1 is also implicated in drug resistance in TNBC. Docetaxel, which stabilizes microtubules by binding to β -tubulin, shows reduced effectiveness in FSIP1-deficient TNBC cells, suggesting that microtubule stability is compromised in the absence of FSIP1 [43,44].”
Understanding the impact of cytoskeleton disruption on synaptic plasticity in Alzheimer’s disease
Basavaraju, K. C., & Priyadarshini, P. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.020 · Cited by 1
Nanoplastics impair neuroimmune integrity via cellular retention and multiple organelle stress
Shahzadi, C., Parekh, P., Batsaikhan, B., Tweedie, D., Costantini, E., Glotfelty, E. J., Carlo, P. D., Reale, M., & Greig, N. H. (2026) · Journal of Hazardous Materials Advances · doi:10.1016/j.hazadv.2026.101380 · Cited by 1
Genomic Copy Number Alterations in Serous Ovarian Cancer
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“LC3B, a ubiquitin-related protein which marks autophagosomal membranes, also acts in microtubule quality control [68].”
Background
Expression profiling of kinesins, involved in the development of autophagy in Arabidopsis thaliana, and the role of tubulin acetylation in the interaction of Atg8 protein with microtubules
Olenieva, V. D., Lytvyn, D. I., Yemets, A. I., & Blume, Y. B. (2018) · Faktori eksperimental noi evolucii organizmiv · doi:10.7124/feeo.v22.942 · Cited by 1
A drug potency signature links progression of chronic lymphocytic leukemia to mitochondria-related stress responses and metabolic reprogramming under hypoxia
Kornblihtt, L. I., Lorenzo, M. C. C., Folgar, M. L. G., Minissale, C., Malusardi, C., Rojas, F., Lombardo, T., & Blanco, G. A. C. (2020) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2020.115016 · Cited by 1
α -tubulin acetylation and detyrosination correlate with starvation-induced autophagy in tobacco cellsPreprint
Lytvyn, D. I., Yemets, A. I., & Blume, Y. B. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/111484 · Cited by 1
“But processes of autophagosome formation are probably more related to dynamic acetylated MTs, whereas autophagosome traffic concerns stable ones (Mackeh et al., 2013).”
Background
Microtubule Defect Involved in ‘Mitophagy Resistance’ Under Subacute Oxidative Stress - Potential Mechanism for Cellular InflammationPreprint
Tamura, T., Yasuda, N., Shakuo, T., Kashiwagi, A., Martyn, J. A. J., Yokoyama, M., & Yasuhara, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.26.966234 · Cited by 1
A conserved microtubule-binding region in Xanthomonas XopL is indispensable for induced plant cell death reactionsPreprint
Ortmann, S., Marx, J., Lampe, C., Ehnert, T.-M., Zinecker, S., Reimers, M., Bonas, U., & Erickson, J. L. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.06.531251 · Cited by 1
“24 from autophagosome biogenesis to transport or docking with the vacuole (42, 44, 45).”
Background
Role of Autophagy in Cancer Therapy
Ma, Y. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802937-4.00013-2
Regulation of Autophagy by Actin-Associated Signaling Pathways
Chan, E. Y. W., & Olson, M. F. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802936-7.00004-0
AMBRA1-Mediated Regulation of C-MYC and Its Relevance to Cancer
Cianfanelli, V., & Cecconi, F. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-812146-7.00018-4
Restoring vascular endothelial autophagic flux reduces atherosclerotic lesionsPreprint
Chatterjee, S., Kheloufi, M., Mazlan, S. M. I., Loyer, X., McKinsey, T. A., Boulanger, C. M., & Coly, P. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.06.442901
Microtubule Targeting Agents Induce ROS–Mediated Apoptosis in Cancer
Das, A. K., Paul, S., Chakrabarty, S., Dasgupta, M., & Chakrabarti, G. (2021) · Springer eBooks · doi:10.1007/978-981-15-4501-6_46-1
Highlighting the hidden: monitoring the avidity-driven association of a fluorescent GABARAP tandem with microtubules in living cells
Üffing, A., Gold, L. H., Gensch, T., Weiergräber, O. H., Hoffmann, S., & Willbold, D. (2024) · Autophagy Reports · doi:10.1080/27694127.2024.2348899
Mitochondrial and Microtubule Defects in Exfoliation GlaucomaPreprint
Venkatesan, A., Ridilla, M., Castro, N., Wolosin, J. M., Henty-Ridilla, J. L., Knox, B. E., Ganapathy, P. S., Brown, J. S., DeVincentis, A. F., Sieminski, S. F., et al. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.5055355
Mitochondrial and Microtubule Defects in Exfoliation GlaucomaPreprint
Venkatesan, A., Ridilla, M., Castro, N., Wolosin, J. M., Henty-Ridilla, J. L., Knox, B. E., Ganapathy, P. S., Brown, J. S., DeVincentis, A. F., Sieminski, S. F., et al. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5114437
Impact of vincristine treatment on the mouse ovary and the potential protective effect of dichloroacetatePreprint
Toledo, A., Simoes, P., Fernández-Tabó, C., Mir, K. H., Chávez‐Genaro, R., & Anesetti, G. (2025) · Research Square · doi:10.21203/rs.3.rs-7254488/v1
Neoliensinine promotes lysosomal cell death in T cell malignancies via a novel STING-TUBA1B pathway
Hu, P., Huang, Y., Yu, Z., Zhang, X., Yang, G., & Yang, P. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101809
“21 Therefore, we pre-treated T-CM cells for 1 h with microtubule destabilizers (colchicine and vinblastine sulfate) and then treated cells for 4 h with 4 μ mol/L of NeoL to examine the effects of microtubules on NeoL-induced STING trafficking.”
MYO5A-mediated stabilization promotes the acquisition of fusion competence in sealed autophagosomes
Nambiar, A., Martin, R., Tomar, K., Knölker, H., Koushika, S. P., Subramaniam, K., & Manjithaya, R. R. (2026) · The EMBO Journal · doi:10.1038/s44318-025-00686-9
“…of autophagosomes toward the lysosome-rich perinuclear region, while kinesins regulate autophagosomal biogenesis by promoting anterograde transport of Atg9 vesicles, as seen with kinesin, UNC-104 in C. elegans (Mackeh et al, 2013; Stavoe et al, 2016; Cason et al, 2022; Cason and Holzbaur, 2023).”
L'alpha-tubuline B et ses régulateurs chez le champignon Botrytis cinerea : régulation, rôles et interactants
Talmey, Y. F. (2014) · theses.fr (ABES) · doi:10.70675/19614ee5zadd0z4838z930cz4ac6a7f7afc4

Authors: Mackeh, R., Perdiz, D., Lorin, S., Codogno, P., & Poüs, C.
Affiliations: Université Paris-Sud (FR)
Inserm (FR)
Corresponding author: Codogno, Patrice
ORCID: Mackeh, Rafah
Perdiz, Daniel
Codogno, Patrice
Poüs, Christian
Venue: Journal of Cell Science
Publisher: The Company of Biologists
Published: 2013-03-01
Volume: 126
Issue: 5
Pages: 1071-1080
ISSN: 0021-9533 (ISSN-L)
1477-9137
DOI: 10.1242/jcs.115626
OpenAlex: W2098921256
Semantic Scholar: bd987f4dde12826f66e2891ff2e65de145d37370
Cited by: 212
References: 110
Citations by year: 2026: 9 · 2025: 12 · 2024: 13 · 2023: 13 · 2022: 20 · 2021: 20 · 2020: 20 · 2019: 21 · 2018: 17 · 2017: 20 · 2016: 16 · 2015: 10 · 2014: 18 · 2013: 3
FWCI: 11.44
Type: journal article
Language: en
Open access: closed
Locations: Journal of Cell Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords: autophagy, microtubules, autophagosome formation, autophagosome transport, autolysosomes, microtubule dynamics, tubulin post-translational modifications, microtubule motor proteins, nutrient deprivation, organelle degradation
MeSH terms: Animals, Autophagy, Humans, Lysosomes, Microtubules, Models, Biological, Phagocytosis, Protein Processing, Post-Translational, Tubulin

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