Proteomics

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LC-MSMS of cell secretome for MAP1LC3B interactors

ABSTRACT: Growing evidence implicates autophagy in cell secretion. Identifying the repertoire of proteins involved with autophagy dependent secretions is key for understanding the underlying mechanism. We use a proximity-dependent biotinylation proteomics strategy to label protein that engage the autophagy regulator MAP1LC3B (LC3/ATG8) in cells; the labeled proteins are then secreted, captured with neutravidin, tryptically digested, and identified by LC-MS/MS. Cells stably expressing BirA* alone serves as control for non-specific cytosolic labeling. SILAC is employed to quantify the degree of LC3B interaction over the background.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture, Fibroblast

DISEASE(S): Disease Free

SUBMITTER: Hector Huang  

LAB HEAD: Arun Paul Wiita

PROVIDER: PXD006541 | Pride | 2022-03-01

REPOSITORIES: Pride

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Publications

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 (  ...[more]

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