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- Jorge Larios
- Department of Biochemistry, Université de Genève, Geneva, Switzerland
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- Vincent Mercier
- Department of Biochemistry, Université de Genève, Geneva, Switzerland
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- Aurélien Roux
- Department of Biochemistry, Université de Genève, Geneva, Switzerland
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- Jean Gruenberg
- Department of Biochemistry, Université de Genève, Geneva, Switzerland
書誌事項
- 公開日
- 2020-02-12
- 権利情報
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- https://creativecommons.org/licenses/by/4.0/
- DOI
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- 10.1083/jcb.201904113
- 公開者
- Rockefeller University Press
この論文をさがす
説明
<jats:p>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.</jats:p>
収録刊行物
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- Journal of Cell Biology
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Journal of Cell Biology 219 (3), e201904113-, 2020-02-12
Rockefeller University Press