期刊
JOURNAL OF CELL BIOLOGY
卷 219, 期 3, 页码 -出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201904113
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资金
- Swiss National Science Foundation
- Swiss Sinergia program
- PolishSwiss Research Program [PSPB-094/2010]
- NCCR in Chemical Biology
- LipidX from the Swiss SystemsX.ch initiative
- Human Frontier Science Program Young Investigator Grant [RGY0076/2009-C]
- Swiss National Fund for Research [31003A_130520, 31003A_149975, 31003A_173087]
- European Research Council [311536]
- Swiss National Science Foundation (SNF) [31003A_130520, 31003A_173087, 31003A_149975] Funding Source: Swiss National Science Foundation (SNF)
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.
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