PXD004582

PXD004582 is an original dataset announced via ProteomeXchange.

Title	Characterization of the acetylome associated with rapamycin-induced autophagy in HeLa cells
Description	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.
HostingRepository	PRIDE
AnnounceDate	2022-03-03
AnnouncementXML	Submission_2022-03-03_02:50:35.154.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Shiping Ding
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	acetylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2016-07-15 01:20:23	ID requested
⏵ 1	2022-03-03 02:50:35	announced

Dataset with its publication pending

curator keyword: Biological

submitter keyword: autophagy

rapamycin

acetylome

acetylation

acetyltransferase

Singping Ding
contact affiliation	Zhejiang University
contact email	dingshiping@zju.edu.cn
lab head
Shiping Ding
contact affiliation	Zhejiang Univesity
contact email	dingshiping@zju.edu.cn
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD004582
     1. Label: PRIDE project
     2. Name: Characterization of the acetylome associated with rapamycin-induced autophagy in HeLa cells