The DOI matches its Crossref record; 216 of the 221 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
Cited by
Sorted by citations
Items 901–960 of 960
Rôle de la méthylation des protéines ESCRT-III dans la régulation de la cytokinèse
Richard, A. (2023) · theses.fr (ABES) · doi:10.70675/4ac53a42zc69az4acdzaa91z4bc3d2b5901e
Gomez-Raya-Vilanova, M. V. (2024) · theses.fr (ABES) · doi:10.70675/426feb97z7f5ez4a21z911ezefbbc5456dc5
Mechanisms of Extracellular Vesicle Cargo Delivery
Askarian‐Amiri, S. (2023) · theses.fr (ABES) · doi:10.70675/7fc22cfaz56eez4b3aza652z01d13ba8b908
Elucidating the Vulnerability of Glioblastoma Stem-like Cells to Lysosomal Dysfunctions
Maghe, C. (2023) · theses.fr (ABES) · doi:10.70675/cb5da8bdzc225z4cf1z80a7zeb24afa442f9
Membrane integrity control – from lipids to proteins and back to lipids
Mu, B., & Zhang, D. (2026) · Journal of Cell Science · doi:10.1242/jcs.264503
Rôle des 2'-O-méthylations internes du génome ARN du VIH-1 dans la réplication virale
Decombe, A. (2023) · theses.fr (ABES) · doi:10.70675/82535ee7z2ed0z457ezb976za900d3f7241a
Langejürgen, A., Schmidt, G., Unsöld, L., Tatge, H., Oyson, E., & Gerhard, R. (2026) · Toxins · doi:10.3390/toxins18040186
Exosomes in Amyloid Propagation—Roles in Neurodegeneration
Mishra, R., & Upadhyay, A. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05913-w
The Pathology of Viral Infections
Veenstra, T. D. (2026) · Advances in experimental medicine and biology · doi:10.1007/978-3-032-22340-1_6
Poulin, K. L., René, C. A., Smith, I. C., Vacratsis, P. O., Burger, D. E., McMillan, H. J., Kothary, R., Perkins, T. J., Warman‐Chardon, J., & Parks, R. J. (2026) · Molecular Therapy Advances · doi:10.1016/j.omta.2026.201757
ESCRT-mediated membrane fission
Tannous, E., Muthukumar, S. S., Audéoud, D., Guilligay, D., & Weissenhorn, W. (2026) · Elsevier eBooks · doi:10.1016/b978-0-323-99507-8.00067-6
Chen, X., Chen, X., Long, Y., Tian, X., Fang, Z., Abubakar, Y. S., Zheng, H., Wang, Z., & Zheng, W. (2026) · New Phytologist · doi:10.1111/nph.71276 · Cited by 1
Chen, Y., Qian, P., Lv, J., Gan, Z., Jiang, D., Xiao, H., Li, R., Zhang, Q., Chen, S., Ping, Y., et al. (2026) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2026.127037
ESCRT proteins organise stress-induced organelle contact between endoplasmic reticulum and GolgiPreprint
Pajonk, O., Albert, L., Schäfer, J. A., de Jager, L., de Hijas, C. M., Papagiannidis, D., Odehnalová, K., Friemel, N., Esch, B. M., Fröhlich, F., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.29.728859
Autophagy in VZV infection: To degrade, or to deliver?
Shen, Z., Xia, N., Cheng, T., & Wang, W. (2026) · Virology · doi:10.1016/j.virol.2026.111001
Liu, H., Zhong, J., Li, X., Bian, C., Ni, Q., Qiu, Y., Qu, L., Cui, L., Wang, Y., Feng, P., et al. (2026) · Nano Today · doi:10.1016/j.nantod.2026.103097
ESCRT: A Cellular Nexus of Plant Immunity and Pathogen Counter‐Strategies
Sexton, W. K., & Xiao, S. (2026) · Molecular Plant Pathology · doi:10.1111/mpp.70298
Shalaby, M. F., McLean, S. L., & Kantamneni, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.17.732891
Nanocondensate tunnellingPreprint
Han, L., Wan, Y., Guo, Z., Gao, S., Wang, H., & Mao, Y. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.22.731667
The kinesin-4 family member KIF27 regulates mitotic progression, cytokinesis and genome stabilityPreprint
Pust, S., Migliano, S. M., Brech, A., Stanciu, S. G., Stenmark, H., & Haglund, K. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.26.734704
Self-citationUnicellular, Collective, and Extended Minds: From Cells to the Biosphere
Miller, W. B., Baluška, F., Slijepčević, P., & Reber, A. S. (2026) · Springer eBooks · doi:10.1007/978-3-032-23779-8_15
Mohamed, L. A. A. H., Shalaby, M. F., Williamson, R., McLean, S. L., & Kantamneni, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.01.735805
Arai, H., Elliott, A., Yang, Y., Farrell, A. P., Millstein, J., Ou, F., Innocenti, F., Wang, J., Battaglin, F., Jayachandran, P., et al. (2026) · Oncogene · doi:10.1038/s41388-026-04019-w
Lv, N., Tang, Y., Zhang, W. K., Zhang, Q., Zhang, H., Gao, H., Cui, S., Krasny, S., & Shi, L. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01823-5
Exosomes Next-Generation Approaches in Breast Cancer: Nano Drug Delivery to AI-Based Prediction
Shah, T. M. (2026) · Journal of Drug Delivery and Therapeutics · doi:10.22270/jddt.v16i7.7891 · Cited by 1
Lavado‐García, J., Bosch-Molist, L., Ruiz-Ayala, C., Jorge, I., Vázquez, J., Gòdia, F., & Cervera, L. (2026) · Molecular Therapy Advances · doi:10.1016/j.omta.2026.201815
胡蓉蓉, Ataullev, Z., & Lou, L. (2026) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70999
Archaeal Diversity Sheds New Light on the Origin of the Eukaryotic Endomembrane System
Lu, Z., Zhang, S., Song, N., Feng, X., Zhou, Z., Liu, Y., & Li, M. (2026) · Annual Review of Microbiology · doi:10.1146/annurev-micro-042524-032136
Ma, J. X., Hu, X., Liu, X., Qi, M., Shi, L., Chen, M., Xie, Y., Wang, B., & Zhou, J. (2026) · Stem Cells · doi:10.1093/stmcls/sxag042
Hu, P., Lu, M., Cassandre, N. H., Chen, P., Liu, H., & Shi, Y. (2026) · Microbiological Research · doi:10.1016/j.micres.2026.128652
A protective ESCRT sleeve for ultrafine DNA bridges
Barral, Y., & Mendoza, M. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01856-x
Gao, H., Luo, X., Fu, Y., Chen, Y., Ning, S.-Y., Han, X., Wang, L., & Wang, Q.-F. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1865003
Initial Molecular Detection of Membrane Damage in Post-Golgi Compartments
Shiba, Y., & Saito, N. (2026) · Cells · doi:10.3390/cells15151375
Romano, J. D., Khan, S. M., & Coppens, I. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1014473
Identification of Yeast Protein Sequences With Similarity to the ESCRT‐III Protein Snf7
Brune, T., & Kölling, R. (2026) · Yeast · doi:10.1002/yea.70040
Sorcin couples Annexin A11 recruitment to ESCRT-III assembly for plasma membrane repair
Ngo, J. M., Williams, J. K., Murugupandiyan, A., & Schekman, R. W. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2610420123 · Cited by 1
The Shape of No Escape: Membrane Self‐Organization Under Confinement
Mayorga, L. S., Mascotti, M. L., & Masone, D. (2026) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.70080
Geller, A., Kwon, M. J., Simmons, S., Xu, Q., Martenis, W. E., Doman, J. L., Natarajan, S., Stalnaker, K. J., Zhang, J., Adiconis, X., et al. (2026) · eLife · doi:10.7554/elife.112104.1
Geller, A., Kwon, M. J., Simmons, S., Xu, Q., Martenis, W. E., Doman, J. L., Natarajan, S., Stalnaker, K. J., Zhang, J., Adiconis, X., et al. (2026) · eLife · doi:10.7554/elife.112104
Ion transport as a determinant of membrane fusion and fission
Levin‐Konigsberg, R., Grinstein, S., & Freeman, S. A. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01860-1
A cellular state-gated model for the biogenesis and function of mitochondrial extracellular vesicles
Zhai, P., Ma, T., Wu, W., Lu, H., Chen, Y., Zhang, T., Peng, Z., Xu, D., & Li, Y. (2026) · Mitochondrion · doi:10.1016/j.mito.2026.102203
A minimal Asgard archaeal ESCRT-III system remodels membranes across scalesPreprint
Schwille, P., Zivkovic, H., Hrebík, D., Frohn, B. P., Basquin, J., Riggi, M., & Briggs, J. A. G. (2026) · Research Square · doi:10.21203/rs.3.rs-10742307/v1
Benoist, M., & Vassilopoulos, S. (2026) · Traffic · doi:10.1111/tra.70053
García-Muñoz, J. I., Domenech‐Bendaña, A., Gimeno-Mallench, L., Ponce‐Mora, A., Fernández, Á. F., López-López, D., Nieto-Torres, J. L., & Bejarano, E. (2026) · International review of cytology · doi:10.1016/bs.ircmb.2026.07.006
Understanding autophagy: A molecular and physiological perspective
Bueno-Arribas, M., Romeo-Guitart, D., & Oury, F. (2026) · International review of cytology · doi:10.1016/bs.ircmb.2026.07.002
Vps4B controls caspase-1 dynamics at the ASC speck to drive inflammasome activation
Li, Y., Xie, Q., Li, L., Mao, R., Yang, L., Liu, X., Gao, C., Man, S. M., Xu, X., Xu, T., et al. (2026) · The Journal of Experimental Medicine · doi:10.1084/jem.20260373
Ma, J., Wang, G., Cai, Y., Feng, K., Wang, X., Lu, M., Zhao, Y., Wu, H., Ge, Z., Ma, M., et al. (2026) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2026.119144
Darvishali, M. H., Rahimmanesh, I., Zaker, E., Nouri, N., Davoodi, A., Pour, F. S., Borzacchiello, A., Choi, Y. J., Gupta, V. K., Khanahmad, H., et al. (2026) · Chemical Engineering Journal · doi:10.1016/j.cej.2026.182065
Beyond efficiency: the AI-driven shift toward safer lipid nanoparticles for gene delivery
Xie, H.-X., Liu, J.-Q., Zhao, M., Zhou, T., Xing, L., Cheng, X. W., Tian, Z., Wang, Y., & Jiang, H. (2026) · Journal of Controlled Release · doi:10.1016/j.jconrel.2026.115364
Guil‐Luna, S., Sánchez-Montero, M. T., Díaz‐Chacón, A., & Rodríguez‐Ariza, A. (2026) · MedComm · doi:10.1002/mco2.70873
Wang, C., Zhang, Y., Zhou, B., Verma, P., Hamera, S., & Zeng, L. (2026) · New Phytologist · doi:10.1111/nph.71590 · Cited by 1
Bi, X., Gootin, H., Su, W., & Baudry, M. (2026) · Bioengineering · doi:10.3390/bioengineering13101140
Pegushin, D. A., Oganesyan, M. V., & Nikolenko, V. N. (2026) · Clinical & Experimental Metastasis · doi:10.1007/s10585-026-10432-y
Huang, Y., Xie, R., Ma, J., & Yu, L. (2026) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-026-01021-8
Ruan, J., Yin, Z., 甘艺荣, Jiang, L., Guo, C., & Yi, P. (2026) · New Phytologist · doi:10.1111/nph.71651
Yang, Y., Liang, J., Wang, L., Zhang, H., Zhang, Z., Liu, Y., Zhu, R., Xu, W., Xu, S., Sun, D., et al. (2026) · Advanced Science · doi:10.1002/advs.78310
Advancing Exosome Research through Artificial Intelligence: Advancements and Applications
Chadha, S. (2026) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/j.jpet.2026.105047
BindingDB Entry 50023196: Insights into tumor-derived exosome inhibition in cancer therapy.
BindingDB (2026) · UC San Diego · doi:10.7270/q25t3rcm
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
