Cited by 324Cellular transport and secretionUbiquitin and proteasome pathwaysAutophagy in Disease and Therapy

ALIX and the multivesicular endosome: ALIX in Wonderland

Bissig, Christin, Gruenberg, Jean·2014·Trends in Cell Biology

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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Crossref · 10.1016/j.tcb.2013.10.009

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66 of 66 references verified0 citation errors · 0 not checkable

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  • LBPA is functionally involved in membrane degradation by recruiting PDCD6IP.

    “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]

  • PDCD6IP binds in a Ca2+-dependent manner to endophilins, which influence endosomal membrane shape probably through interaction with dynamin via SH3 domains.

    “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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Authors
Bissig, C., & Gruenberg, J.
Affiliations
University of Geneva (CH)
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
  • Health Sciences › Medicine › Epidemiology › 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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