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The LC3-conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles.
Nature Cell Biology ( IF 20.042 ) Pub Date : 2020-01-13 , DOI: 10.1038/s41556-019-0450-y
Andrew M Leidal,Hector H Huang,Timothy Marsh,Tina Solvik,Dachuan Zhang,Jordan Ye,FuiBoon Kai,Juliet Goldsmith,Jennifer Y Liu,Yu-Hsin Huang,Teresa Monkkonen,Ariadne Vlahakis,Eric J Huang,Hani Goodarzi,Li Yu,Arun P Wiita,Jayanta Debnath

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.
更新日期:2020-01-14

 

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