PXD029481

PXD029481 is an original dataset announced via ProteomeXchange.

Title	Quantitative Proteomics Analysis Expands the Roles of Lysine -Hydroxybutyrylation Pathway in Response to Environmental β-Hydroxybutyrate
Description	Lysine -hydroxybutyrylation (Kbhb) is a newly identified protein post-translational modification that derived from the ketone body β-hydroxybutyrate (BHB). BHB is synthesized in the liver from fatty acids and could be delivered to peripheral tissues when the supply of glucose is too low for the body’s energetic needs. The plasma concentration of BHB can increase up to 20 mM during starvation and in pathological conditions. Despite the progresses, how the cells that do not produce BHB respond to elevated environmental BHB remains largely unknown. Given that BHB significantly drives Kbhb, here we performed a quantitative proteomics study to characterize the BHB-induced lysine -hydroxybutyrylome and acetylome. A total of 840 unique Kbhb sites across 429 proteins were identified, with 42 sites from 39 proteins being increased by more than 50% in response to BHB. The upregulated β-hydroxybutyrylome induced by BHB are involved in aminoacyl-tRNA biosynthesis, 2-oxocarboxylic acid metabolism, citrate cycle (TCA cycle), glycolysis/gluconeogenesis, and pyruvate metabolism pathways. Moreover, some BHB-targeted Kbhb substrates are potentially linked to diseases such as cancer. Taken together, this study revealed the dynamics of lysine -hydroxybutyrylome and acetylome in response to environmental BHB, which sheds light on the roles for Khib in regulation of diverse cellular processes and provides new insights into the biological functions of BHB.
HostingRepository	PRIDE
AnnounceDate	2022-05-25
AnnouncementXML	Submission_2022-05-25_07:08:56.559.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	He Huang
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	acetylated residue
Instrument	timsTOF Pro

Revision	Datetime	Status	ChangeLog Entry
0	2021-11-01 08:53:44	ID requested
⏵ 1	2022-05-25 07:08:57	announced

Hou W, Liu G, Ren X, Liu X, He L, Huang H, -Hydroxybutyrate. Oxid Med Cell Longev, 2022():4592170(2022) [pubmed]

submitter keyword: Posttranslational modification

Lysine -hydroxybutyrylation

Lysine acetylation

Quantitative proteomics

Substrate

He Huang
contact affiliation	Shanghai Institute of Materia Medica
contact email	hhuang@simm.ac.cn
lab head
He Huang
contact affiliation	Shanghai Institute of Materia Medica
contact email	hhuang.nu@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD029481
     1. Label: PRIDE project
     2. Name: Quantitative Proteomics Analysis Expands the Roles of Lysine -Hydroxybutyrylation Pathway in Response to Environmental β-Hydroxybutyrate