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The LC3 conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles (lrgRNA-seq dataset)

ABSTRACT: We employed RNA sequecing to profile large RNAs (mRNAs and lincRNAs) packaged into extracellular vesicles (EVs) from WT cells and cells deficient for the LC3 conjugation machinery

ORGANISM(S): Homo sapiens

PROVIDER: GSE137616 | GEO | 2019/12/26

REPOSITORIES: GEO

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The LC3 conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles (smRNA-seq dataset)

Project description:We employed small non-coding RNA sequecing to profile the small RNAs in extracellular vesicles (EVs) from WT cells and cells deficient for the LC3 conjugation machinery

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The LC3 conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles

Project description:The LC3 conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles

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The LC3-conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles.

Project description:Traditionally viewed as an autodigestive pathway, autophagy also facilitates cellular secretion; however, the mechanisms underlying these processes remain unclear. Here, we demonstrate that components of the autophagy machinery specify secretion within extracellular vesicles (EVs). Using a proximity-dependent biotinylation proteomics strategy, we identify 200 putative targets of LC3-dependent secretion. This secretome consists of a highly interconnected network enriched in RNA-binding proteins (RBPs) and EV cargoes. Proteomic and RNA profiling of EVs identifies diverse RBPs and small non-coding RNAs requiring the LC3-conjugation machinery for packaging and secretion. Focusing on two RBPs, heterogeneous nuclear ribonucleoprotein K (HNRNPK) and scaffold-attachment factor B (SAFB), we demonstrate that these proteins interact with LC3 and are secreted within EVs enriched with lipidated LC3. Furthermore, their secretion requires the LC3-conjugation machinery, neutral sphingomyelinase 2 (nSMase2) and LC3-dependent recruitment of factor associated with nSMase2 activity (FAN). Hence, the LC3-conjugation pathway controls EV cargo loading and secretion.

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The LC3 conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles (smRNA-seq dataset)

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Project description:The LC3 conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles (lrgRNA-seq dataset)

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The LC3 conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles

Project description:This SuperSeries is composed of the SubSeries listed below.

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Secretory autophagy mediates mitochondria clearance in the absence of the mATG8-conjugation machinery

Project description:PINK1-Parkin mediated mitophagy, a selective form of autophagy, represents an important mechanism in mitochondrial quality control (MQC) via clearance of damaged mitochondria. Although it is well known that the conjugation of mammalian ATG8s to phosphatidylethanolamine (PE) is a key step in autophagy, its role in mitophagy remains controversial. In this study, we attempted to clarify the role of the mATG8-conjugation system in mitophagy by generating knockouts of the mATG8-conjugation machinery. Unexpectedly, we show that mitochondria could still be cleared in the absence of mATG8 lipidation, in a process that was found to be independent of lysosomal degradation. Instead, mitochondria were found to be cleared via a secretory autophagy pathway, resulting in the extracellular release of mitochondria, in a process we defined as autophagic secretion of mitochondria (ASM). Functionally, increased ASM promoted the activation of the innate immune cGAS-STING pathway in recipient cells. Overall, data from this study reveal ASM as a novel mechanism in MQC, especially when the cellular mATG8-conjugation machinery is dysfunctional.

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Conjugation-based genome engineering in Deinococcus radiodurans

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