期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 17, 页码 11649-11661出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.445304
关键词
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资金
- Instituto de Salud Carlos III [PI080794, PI11/01645]
- Ministerio de Ciencia e Innovacion (MCINN) [ERC-2011-AdG 294340-GEN-TRIS, SAF2011-25834]
- Comunidad de Madrid (CAM) [INDISNET S2011/BMD-2332]
- MCINN [BIO2009-07990]
- CAM [BIO/0194/2006]
- Fondo de Investigaciones Sanitarias (MCINN) [RECAVA RD06/0014]
Extracellular vesicles are emerging as a potent mechanism of intercellular communication because they can systemically exchange genetic and protein material between cells. Tetraspanin molecules are commonly used as protein markers of extracellular vesicles, although their role in the unexplored mechanisms of cargo selection into exosomes has not been addressed. For that purpose, we have characterized the intracellular tetraspanin-enriched microdomain (TEM) interactome by high throughput mass spectrometry, in both human lymphoblasts and their derived exosomes, revealing a clear pattern of interaction networks. Proteins interacting with TEM receptors cytoplasmic regions presented a considerable degree of overlap, although some highly specific CD81 tetraspanin ligands, such as Rac GTPase, were detected. Quantitative proteomics showed that TEM ligands account for a great proportion of the exosome proteome and that a selective repertoire of CD81-associated molecules, including Rac, is not correctly routed to exosomes in cells from CD81-deficient animals. Our data provide evidence that insertion into TEM may be necessary for protein inclusion into the exosome structure.
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