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ALIX- and ESCRT-III-dependent sorting of tetraspanins to exosomes.

  • Larios J Department of Biochemistry, Université de Genève, Geneva, Switzerland.
  • Mercier V Department of Biochemistry, Université de Genève, Geneva, Switzerland.
  • Roux A Department of Biochemistry, Université de Genève, Geneva, Switzerland.
  • Gruenberg J Department of Biochemistry, Université de Genève, Geneva, Switzerland.
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  • 2020-02-13
Published in:
  • The Journal of cell biology. - 2020
Calcium-Binding Proteins
Cell Cycle Proteins
Endosomal Sorting Complexes Required for Transport
Endosomes
Exosomes
HeLa Cells
Humans
Lysophospholipids
Monoglycerides
Protein Transport
Tetraspanin 28
Tetraspanin 29
Tetraspanin 30
Tetraspanins
Time Factors
English The intraluminal vesicles (ILVs) of endosomes mediate the delivery of activated signaling receptors and other proteins to lysosomes for degradation, but they also modulate intercellular communication when secreted as exosomes. The formation of ILVs requires four complexes, ESCRT-0, -I, -II, and -III, with ESCRT-0, -I, and -II presumably involved in cargo sorting and ESCRT-III in membrane deformation and fission. Here, we report that an active form of the ESCRT-associated protein ALIX efficiently recruits ESCRT-III proteins to endosomes. This recruitment occurs independently of other ESCRTs but requires lysobisphosphatidic acid (LBPA) in vivo, and can be reconstituted on supported bilayers in vitro. Our data indicate that this ALIX- and ESCRT-III-dependent pathway promotes the sorting and delivery of tetraspanins to exosomes. We conclude that ALIX provides an additional pathway of ILV formation, secondary to the canonical pathway, and that this pathway controls the targeting of exosomal proteins.
Language
  • English
Open access status
gold
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Persistent URL
https://sonar.rero.ch/global/documents/215844
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