Characterization of the acetylome associated with rapamycin-induced autophagy in HeLa cells

ABSTRACT: Autophagy is a lysosomal-mediated catabolic process that degrades cytoplasmic components to help maintain cellular homeostasis and cell survival during exposure to stress. Lysine acetylation is a reversible post-translational modification that plays an important role in the regulation of diverse cellular processes. In this study, by using stable isotope labeling by amino acids in cell culture (SILAC)-based quantitative proteomics analysis, we explored lysine acetylomics in response to rapamycin-induced autophagy in HeLa cells. In total, we identified 1,808 acetylation sites on 944 proteins, among which, significant changes of lysine acetylation on 533 sites on 397 proteins were observed. The identified lysine acetylated proteins were mainly distributed in the cytoplasm, nucleus and mitochondria. FxK*, K*xxxxK and KxxxxK* were shown to be potential autophagy-related lysine acetylated motifs. Gene Ontology enrichment analysis showed that all of the significantly acetylated proteins were involved in diverse transcription-dependent and independent pathways. Further analysis found that acetylation was significantly enriched in three major metabolic processes. Moreover, Several protein complexes, such as ribosomes, RNA spliceosomes and the ubiquitin-proteasome complex, were also significantly acetylated. Moreover, as expected, significant changes of variations were observed in the acetylation levels of lysine acetylation in acetyltransferases and deacetylases, such as KAT7 and p300, were observed in response to rapamycin-induced autophagy. Taken together, our data are the first to these data reveal that the lysine acetylation associates acetylome associated with autophagy, and therefore to provide new insights into exploring the mechanism of autophagy.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Shiping Ding  

LAB HEAD: Singping Ding

PROVIDER: PXD004582 | Pride | 2022-03-03

REPOSITORIES: Pride