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The many functions of ESCRTs
Abstract
Cellular membranes can form two principally different involutions, which either exclude or contain cytosol. The 'classical' budding reactions, such as those occurring during endocytosis or formation of exocytic vesicles, involve proteins that assemble on the cytosol-excluding face of the bud neck. Inverse membrane involution occurs in a wide range of cellular processes, supporting cytokinesis, endosome maturation, autophagy, membrane repair and many other processes. Such inverse membrane remodelling is mediated by a heteromultimeric protein machinery known as endosomal sorting complex required for transport (ESCRT). ESCRT proteins assemble on the cytosolic (or nucleoplasmic) face of the neck of the forming involution and cooperate with the ATPase VPS4 to drive membrane scission or sealing. Here, we review similarities and differences of various ESCRT-dependent processes, with special emphasis on mechanisms of ESCRT recruitment.
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“This final event is carried out by the ESCRT-III membrane scission machinery that is recruited by ALIX and ESCRT-I to these scission sites (for review, see [16]).”
From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [16]
In the citing paper
“A series of multi-protein ESCRT complexes (endosomal sorting complexes required for transport) recognise cargo modified through monoubiquitylation and transport these for degradation within the lysosome7.”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [7]
Citations
Cites
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
Shedding light on the cell biology of extracellular vesicles
van Niel, G., D'Angelo, G., & Raposo, G. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.125 · Cited by 8,369
Syndecan–syntenin–ALIX regulates the biogenesis of exosomes
Baietti, M. F., Zhang, Z., Mortier, E., Melchior, A., Degeest, G., Geeraerts, A., Ivarsson, Y., Depoortere, F., Coomans, C., Vermeiren, E., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2502 · Cited by 1,899
Katzmann, D. J., Babst, M., & Emr, S. D. (2001) · Cell · doi:10.1016/s0092-8674(01)00434-2 · Cited by 1,473
Itakura, E., Kishi‐Itakura, C., & Mizushima, N. (2012) · Cell · doi:10.1016/j.cell.2012.11.001 · Cited by 1,385
Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
Garrus, J. E., von Schwedler, U. K., Pornillos, O. W., Morham, S. G., Zavitz, K. H., Wang, H. E., Wettstein, D. A., Stray, K. M., Côté, M., Rich, R. L., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00506-2 · Cited by 1,369
The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
Raiborg, C., & Stenmark, H. (2009) · Nature · doi:10.1038/nature07961 · Cited by 1,359
Self-citationNuclear envelope rupture and repair during cancer cell migration
Denais, C. M., Gilbert, R. M., Isermann, P., McGregor, A. L., te Lindert, M., Weigelin, B., Davidson, P. M., Friedl, P., Wolf, K., & Lammerding, J. (2016) · Science · doi:10.1126/science.aad7297 · Cited by 1,318
DNA breaks and chromosome pulverization from errors in mitosis
Crasta, K., Ganem, N. J., Dagher, R., Lantermann, A. B., Ivanova, E. V., Pan, Y., Nezi, L., Protopopov, A., Chowdhury, D., & Pellman, D. (2012) · Nature · doi:10.1038/nature10802 · Cited by 1,227
Gibbings, D., Ciaudo, C., Erhardt, M., & Voinnet, O. (2009) · Nature Cell Biology · doi:10.1038/ncb1929 · Cited by 1,037
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Guo, W., Zhou, H., Wang, J., Lu, J., Dong, Y., Kang, Z., Qiu, X., Ouyang, X., Chen, Q., Li, J., et al. (2024) · Advanced Science · doi:10.1002/advs.202308307 · Cited by 34
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Elias, R. D., Ma, W., Ghirlando, R., Schwieters, C. D., Reddy, V. S., & Deshmukh, L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010635117 · Cited by 36
Liese, S., Wenzel, E. M., Kjos, I., Molina, R. R., Schultz, S. W., Brech, A., Stenmark, H., Raiborg, C., & Carlson, A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2014228117 · Cited by 34
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Sun, F., Sun, Y., Wu, F., Xu, W., & Qian, H. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14102208 · Cited by 40
Wang, C., Li, W., Shao, L., Zhou, A., Zhao, M., Li, P., Zhang, Z., & Wu, J. Q. (2023) · European journal of medical research · doi:10.1186/s40001-023-01458-z · Cited by 34
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Rose, K. M., Hirsch, V. M., & Bouamr, F. (2020) · Viruses · doi:10.3390/v12101188 · Cited by 32
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Ofori, K., Bhagat, G., & Rai, A. J. (2020) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.14611 · Cited by 31
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Simões, S. D. M., Lerchbaumer, G., Pellikka, M., Giannatou, P., Lam, T., Kim, D.-H., Yu, J. C., ter Stal, D., Kakouni, K. A., Fernández‐González, R., et al. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202108076 · Cited by 23
Mayoral, J., Guevara, R. B., Rivera-Cuevas, Y., Tu, V., Tomita, T., Romano, J. D., Gunther-Cummins, L., Sidoli, S., Coppens, I., Carruthers, V. B., et al. (2022) · mBio · doi:10.1128/mbio.01442-22 · Cited by 25
Ruan, Z., Liang, Y., Chen, Z., Yin, J., Li, C., Pan, P., Zhang, Q., Wu, J., & Luo, Z. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1024899 · Cited by 26
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Okamura, A., Yoshioka, Y., Saito, Y., & Ochiya, T. (2022) · Pharmaceutical Research · doi:10.1007/s11095-022-03463-z · Cited by 25
Hattori, T., Fundora, K. A., Hamamoto, K., Opozda, D. M., Liang, X., Liu, X., Zhang, J., Uzun, Y., Takahashi, Y., & Wang, H. (2023) · Autophagy · doi:10.1080/15548627.2023.2258701 · Cited by 24
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coordination, O., Elsasser, S., Elia, L. P., Morimoto, R. I., Powers, E. T., Elsasser, S., Finley, D. J., Costa, B., Budron, M., Tokuno, Z., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.22.533675 · Cited by 32
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Metadata
- Authors
- Vietri, M., Radulovic, M., & Stenmark, H.
- Affiliations
- Oslo University Hospital (NO)
- Corresponding author
- Stenmark, Harald
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2019-11-08
- Volume
- 21
- Issue
- 1
- Pages
- 25-42
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2985101511
- Cited by
- 962
- References
- 221
- Citations by year
- 2026: 117 · 2025: 159 · 2024: 165 · 2023: 144 · 2022: 150 · 2021: 152 · 2020: 74 · 2019: 1
- FWCI
- 10.94
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- ESCRT, membrane fission, membrane sealing, cytokinesis, endosome maturation, autophagy, membrane repair, viral replication, budding
- MeSH terms
- Spastin, Animals, Cell Membrane, Humans, Neurons, Nuclear Envelope, Phagosomes, Endosomes, Virus Replication, Protein Transport, Cytokinesis, Host-Pathogen Interactions, Exosomes, Endosomal Sorting Complexes Required for Transport
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