Histone lactylation: epigenetic mark of glycolytic switch
No Thumbnail Available
File version
Author(s)
Dai, X
Lv, X
Thompson, EW
Ostrikov, K
Lv, X
Thompson, EW
Ostrikov, K
Griffith University Author(s)
Primary Supervisor
Other Supervisors
Editor(s)
Date
2021
Size
File type(s)
Location
License
Abstract
Histone lactylation and acetylation compete for epigenetic modification of lysines and mark the levels of lactates and acetyl-CoA. Whether pyruvate is committed to lactate or acetyl-CoA generation as the outlet of glycolysis determines cell fate towards malignancy or not. Taking control over the glycolytic switch as marked by lactylation suggests novel therapeutic opportunities against cancers.
Journal Title
Trends in Genetics
Conference Title
Book Title
Edition
Volume
Issue
Thesis Type
Degree Program
School
Publisher link
Patent number
Funder(s)
Grant identifier(s)
Rights Statement
Rights Statement
Item Access Status
Note
This publication has been entered as an advanced online version in Griffith Research Online.
Access the data
Related item(s)
Subject
Genetics
Glycobiology
Persistent link to this record
Citation
Dai, X; Lv, X; Thompson, EW; Ostrikov, K, Histone lactylation: epigenetic mark of glycolytic switch, Trends in Genetics, 2021