ArticleStructure (London, England : 1993)2009
A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
85 citing papers in PubMed, 130 citations in OpenAlex.
- ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026Review
- The hepatocyte traffic network in the human hepatitis A virus biological cycle from an evolutionary perspective.Communications biology · 2025Article
- Article
- Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair.Nature structural & molecular biology · 2025Article
- NEDD4 family ubiquitin ligase AIP4 interacts with Alix to enable HBV naked capsid egress in an Alix ubiquitination-independent manner.PLoS pathogens · 2024Article
- Article
- Palmitoylation of vacuole membrane protein 1 promotes small extracellular vesicle secretion via interaction with ALIX and influences intercellular communication.Cell communication and signaling : CCS · 2024Article
- Article
- SUMOylation-triggered ALIX activation modulates extracellular vesicles circTLCD4-RWDD3 to promote lymphatic metastasis of non-small cell lung cancer.Signal transduction and targeted therapy · 2023Article
- UMAD1 contributes to ESCRT-III dynamic subunit turnover during cytokinetic abscission.Journal of cell science · 2023Article
- The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division.Science advances · 2023Article
- In vitro reconstitution of calcium-dependent recruitment of the human ESCRT machinery in lysosomal membrane repair.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Plant ESCRT protein ALIX coordinates with retromer complex in regulating receptor-mediated sorting of soluble vacuolar proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization.BMC biology · 2021Article
- HIV-1 Gag release from yeast reveals ESCRT interaction with the Gag N-terminal protein region.The Journal of biological chemistry · 2020Article
- Article
- Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation.Nature communications · 2020Article
- Article
- ALIX- and ESCRT-III-dependent sorting of tetraspanins to exosomes.The Journal of cell biology · 2020Article
- Changes in ESCRT-III filament geometry drive membrane remodelling and fission in silico.BMC biology · 2019Article
25 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors at 7 institutions in 3 countries.
Funding
Abstract
ALIX recruits ESCRT-III CHMP4 and is involved in membrane remodeling during endosomal receptor sorting, budding of some enveloped viruses, and cytokinesis. We show that ALIX dimerizes via the middle domain (ALIX(-V)) in solution. Structural modeling based on small angle X-ray scattering (SAXS) data reveals an elongated crescent-shaped conformation for dimeric ALIX lacking the proline-rich domain (ALIX(BRO1-V)). Mutations at the dimerization interface prevent dimerization and induce an open elongated monomeric conformation of ALIX(-V) as determined by SAXS modeling. ALIX dimerizes in vivo and dimeric ALIX colocalizes with CHMP4B upon coexpression. We show further that ALIX dimerization affects HIV-1 budding. C-terminally truncated activated CHMP4B retaining the ALIX binding site forms linear, circular, and helical filaments in vitro, which can be bridged by ALIX. Our data suggest that dimeric ALIX represents the active form that interacts with ESCRT-III CHMP4 polymers and functions as a scaffolding protein during membrane remodeling processes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.