The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.
ALIX and the multivesicular endosome: ALIX in Wonderland
Abstract
In yeast and mammalian cells, endosomal sorting complexes required for transport (ESCRT) assist in sorting ubiquitinated proteins into intralumenal vesicles (ILVs) of multivesicular endosomes (MVEs) for degradation in the lysosome/vacuole. In mammalian cells, ESCRTs also drive other topologically identical membrane deformation processes, including cytokinesis, exosome release, and virus budding. Although the ESCRT-associated protein ALIX regulates these mammalian cell-specific functions, it was believed to be dispensable for receptor sorting into ILVs, unlike its yeast homolog Bro1. Despite these differences, recent evidence suggests ALIX and Bro1 share common properties in cargo sorting and ILV formation. We review these commonalities and discuss the role of ALIX in operating 'behind the mirror' during ILV back-fusion with the limiting membrane. We also propose models of how ALIX and some ESCRTs regulate the back-fusion process.
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“LBPA is also functionally involved in membrane degradation by recruiting the programmed cell death-6-interacting protein (PDCD6IP) (45, 46).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [46]
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“PDCD6IP also binds in a Ca2+-dependent manner to endophilins, which influence the endosomal membrane shape (bending) probably through interaction with dynamin via SH3 domains (46).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [46]
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Extracellular vesicles as drug delivery systems: Why and how?
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Macrophage defense mechanisms against intracellular bacteria
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Metadata
- Authors
- Bissig, C., & Gruenberg, J.
- Affiliations
- University of Geneva (CH)
- ORCID
- Gruenberg, Jean
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2014-01
- Volume
- 24
- Issue
- 1
- Pages
- 19-25
- ISSN
- 0962-8924 (ISSN-L)
- OpenAlex
- W2154203178
- Cited by
- 323
- References
- 66
- Citations by year
- 2026: 16 · 2025: 21 · 2024: 29 · 2023: 19 · 2022: 20 · 2021: 29 · 2020: 35 · 2019: 28 · 2018: 33 · 2017: 18 · 2016: 36 · 2015: 24 · 2014: 15
- FWCI
- 2.88
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in 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 › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- Alix, multivesicular endosomes, ESCRT, intralumenal vesicles, ubiquitin-dependent protein degradation, membrane deformation, limiting membrane, exosome secretion, viral budding, cytokinesis
- MeSH terms
- Animals, Calcium-Binding Proteins, Cell Membrane, Humans, Cell Cycle Proteins, Protein Transport, Transport Vesicles, Saccharomyces cerevisiae Proteins, Endosomal Sorting Complexes Required for Transport, Multivesicular Bodies, Ubiquitinated Proteins
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