Proteomics

Dataset Information

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Circadian Regulation of Protein Cargo in Exosomes


ABSTRACT: The circadian clock controls many aspects of physiology, but it remains undescribed whether extracellular vesicles (including exosomes) involved in cell-cell communications between tissues are regulated in a circadian pattern. We demonstrate a 24 h rhythmic abundance of individual proteins in exosomes using liquid chromatography-mass spectrometry in circadian-synchronised tendon fibroblasts. Further, the release of exosomes enriched in RNA-binding proteins was temporally separated from those enriched in cytoskeletal and matrix proteins, which peaked during the end of the light phase. Finally, we targeted the protein sorting mechanism in the exosome biogenesis pathway and established (by knockdown of circadian-regulated flotillin-1) that matrix metalloproteinase 14 abundance in tendon fibroblast exosomes is under flotillin-1 regulation. In conclusion, we have identified proteomic time signatures for exosomes released by tendon fibroblasts which supports the view that the circadian clock regulates protein cargo in exosomes involved in cell-cell crosstalk.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Erwin Schoof  

LAB HEAD: Michael Kjaer

PROVIDER: PXD022393 | Pride | 2022-05-19

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
20190517_FS_Chloe_TimeSeries.pdResult Other
20190517_FS_ES_Chloe_12h_1.raw Raw
20190517_FS_ES_Chloe_16h_1.raw Raw
20190517_FS_ES_Chloe_20h_1.raw Raw
20190517_FS_ES_Chloe_24h_1.raw Raw
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Publications


The circadian clock controls many aspects of physiology, but it remains undescribed whether extracellular vesicles (EVs), including exosomes, involved in cell-cell communications between tissues are regulated in a circadian pattern. We demonstrate a 24-hour rhythmic abundance of individual proteins in small EVs using liquid chromatography-mass spectrometry in circadian-synchronized tendon fibroblasts. Furthermore, the release of small EVs enriched in RNA binding proteins was temporally separated  ...[more]

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