Exosomes contain ubiquitinated proteins

Buschow, Sonja I.; Liefhebber, Jolanda M. P.; Wubbolts, Richard; Stoorvogel, Willem

doi:10.1016/j.bcmd.2005.08.005

Cited by 155 publications

(125 citation statements)

References 37 publications

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“…This hypothesis is supported by the recent detection of ubiquitin in exosomes (20) and previous studies that documented ubiquitin within the lumen of MVBs and lysosomes (21,22). Initial observations with immunofluorescence microscopy using antibodies to LAMP1 and to ubiquitin indicated that there was significant overlap between LAMP1-positive and ubiquitinpositive compartments in both resting BMM⌽s as well as BMM⌽s stimulated into autophagy by starvation [supporting information (SI) Fig.…”

Section: Resultssupporting

confidence: 57%

Lysosomal killing ofMycobacteriummediated by ubiquitin-derived peptides is enhanced by autophagy

Alonso

Pethe

Russell

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

297

277

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Mycobacterium tuberculosis parasitizes resting macrophages yet is killed by activated macrophages through both oxidative and nonoxidative mechanisms. Nonoxidative mechanisms are linked to the maturation of the bacteria-containing phagosome into an acidified, hydrolytically active compartment. We describe here a mechanism for killing Mycobacteria in the lysosomal compartment through the activity of peptides generated by the hydrolysis of ubiquitin. The induction of autophagy in infected macrophages enhanced the delivery of ubiquitin conjugates to the lysosome and increased the bactericidal capacity of the lysosomal soluble fraction. The accumulation of ubiquitinated proteins in the autophagolysosome provides one possible mechanism behind the antimicrobial activities observed for a range of pathogens in autophagous host cells.macrophage ͉ phagosome ͉ tuberculosis ͉ lysosome

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Section: Resultssupporting

confidence: 57%

Lysosomal killing ofMycobacteriummediated by ubiquitin-derived peptides is enhanced by autophagy

Alonso

Pethe

Russell

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

297

277

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“…However, mono and poly-ubiquitinated proteins can be found in exosomes, but not associated to the exosomal membrane [57]. Cargo deubiquitination before its packaging into ILVs seems essential, but how some ubiquitinated proteins end up in exosomes remains controversial.…”

Section: Escrt-dependent and Independent Sorting Mechanisms Into Ilvsmentioning

confidence: 99%

“…Specific antibodies for ubiquitin and poly-ubiquitin chains allowed to identify mono-, oligoand poly-ubiquitinated proteins in exosomes [57]. Various studies and proteomic analysis identified specific ubiquitinated proteins (reviewed in [73]) ( Table 2 and Fig.…”

Section: Ubiquitinated Proteins In Evsmentioning

confidence: 99%

Post-translational add-ons mark the path in exosomal protein sorting

Moreno-Gonzalo

Fernández-Delgado

Sánchez‐Madrid

2017

Cell. Mol. Life Sci.

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“…Exosomes have a characteristic buoyant density and contain a discrete set of proteins, which makes them distinguishable from vesicles released by apoptotic cells (1). Although the exact mechanism of protein sorting into exosomes is poorly defined, it may involve ubiquitination and the ESCRT complex (2,3). Exosomes originating from B cells, T cells, dendritic cells (DC), 3 and mast cells can confer immunoregulatory signals between cells in either an immunostimulatory or suppressive manner.…”

mentioning

confidence: 99%

“…Although the exact mechanism of protein sorting into exosomes is poorly defined, it may involve ubiquitination and the ESCRT complex (2,3). Exosomes originating from B cells, T cells, dendritic cells (DC), 3 and mast cells can confer immunoregulatory signals between cells in either an immunostimulatory or suppressive manner. Indeed, exosomes derived from leukocytes contain many of the important regulatory molecules to carry out this function, such as MHC class I and II, CD80, and CD86, as well as various adhesion molecules that may target exosomes to their acceptor cells (4).…”

mentioning

confidence: 99%

MHC Class II+ Exosomes in Plasma Suppress Inflammation in an Antigen-Specific and Fas Ligand/Fas-Dependent Manner

Kim

Bianco²,

Shufesky

et al. 2007

The Journal of Immunology

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Exosomes are 50- to 100-nm vesicles that are formed within the late endocytic compartment and released from a variety of cell types. Previously, we demonstrated that exosomes derived from dendritic cells transduced with adenoviral vectors expressing IL-10, IL-4, or Fas ligand (FasL) produce anti-inflammatory exosomes able to reduce inflammation in a murine paw delayed-type hypersensitivity model, suppress the onset on murine collagen-induced arthritis, and reduce the severity of established collagen-induce arthritis. In this study, we examined the ability of endogenous, blood-borne exosomes to regulate the immune response. Exosomes isolated from plasma of mice immunized to keyhole limpet hemocyanin, but not from naive or OVA-immunized mice, were able to suppress the keyhole limpet hemocyanin-specific delayed-type hypersensitivity inflammatory response. The anti-inflammatory effect was mediated by MHC class II+ plasma exosomes that were also FasL+ and CD11b+, but CD11c−. Moreover, the anti-inflammatory effect of the MHC class II+ plasma-derived exosomes was, in part, dependent upon the presence of FasL in the exosomes and Fas in the recipient mouse. These results suggest that exosomes in the plasma, produced by MHC class II+ and CD11b+ cells, have the ability to suppress the immune response in an Ag-specific manner in part through a Fas/FasL-dependent manner.

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Exosomes contain ubiquitinated proteins

Cited by 155 publications

References 37 publications

Lysosomal killing ofMycobacteriummediated by ubiquitin-derived peptides is enhanced by autophagy

Lysosomal killing ofMycobacteriummediated by ubiquitin-derived peptides is enhanced by autophagy

Post-translational add-ons mark the path in exosomal protein sorting

MHC Class II+ Exosomes in Plasma Suppress Inflammation in an Antigen-Specific and Fas Ligand/Fas-Dependent Manner

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