期刊
EMBO JOURNAL
卷 25, 期 1, 页码 1-12出版社
WILEY
DOI: 10.1038/sj.emboj.7600759
关键词
annexin 1; EGF; endocytosis; lysobisphosphatidic acid; multivesicular endosome
资金
- MRC [G0100200] Funding Source: UKRI
- Medical Research Council [G0100200] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
- Medical Research Council [G0100200] Funding Source: researchfish
Here we show that EGF and EGF receptor ( EGFR) are trafficked through a subpopulation of multivesicular endosomes/ bodies (MVBs) that are distinct from morphologically identical vacuoles that label for the late endosomal marker lyso-bisphosphatidic acid ( LBPA). EGF stimulation increases both MVB biogenesis and inward vesiculation within EGFR-containing MVBs. Deletion of annexin 1, a substrate of EGFR tyrosine kinase, abolishes the effect of EGF stimulation on inward vesiculation. This phenotype is reversible by transfection with wild-type but not Y21F phosphorylation mutant annexin 1. Deletion of annexin 1 has no effect on EGF-stimulated MVB biogenesis, suggesting that MVB biogenesis and inward vesiculation within MVB are mediated by separate mechanisms. Loss or depletion of annexin 1 has no effect on EGF degradation and causes only a small delay in EGFR degradation, indicating that annexin 1 operates downstream of Hrs- and ESCRT-mediated sorting and is required solely for EGF-stimulated inward vesiculation. Annexin 1 accumulates on internal vesicles of MVB after EGF-stimulated inward vesiculation, suggesting that it may be required for a late stage in inward vesiculation.
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