IndraLab

Statements


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sparser
"Histone lactylation can also enhance USP39 expression, which interacts with the key glycolytic enzyme phosphoglycerate kinase 1 (PGK1) to promote its stability and deubiquitination, thereby increasing PGK1’s biological activity and potentially accelerating the glycolytic pathway."

sparser
"For example, in bladder cancer, H3K18 lactylation promotes tumorigenesis by enhancing the expression of the oncogene Lipocalin-2 (LCN2) ( xref ); in endometrial cancer, histone lactylation upregulates USP39 expression, which further interacts with PGK1 to activate the PI3K/AKT/HIF-1α signaling pathway, accelerating tumor progression ( xref ); in colorectal cancer, the activation of G-protein coupled receptor 37 (GPR37) promotes the expression of LDHA by activating the Hippo pathway, thereby intervening in tumor progression ( xref )."

No evidence text available

sparser
"A reciprocal IP experiment and a reciprocal assay confirmed that PGK1 and USP39 interacted with each other."

sparser
"USP39 interacts with PGK1, thereby activating the PI3K/AKT/HIF-1α signaling pathway, enhancing glycolysis and lactylation, and establishing a carcinogenic positive feedback cycle ( xref ) ( xref )."

sparser
"Researchers have identified the interaction between USP39 and PGK1 using Co-IP and mass spectrometry(MS), and the downregulation of USP39 leads to a decrease in PGK1 protein levels in EC cells."

sparser
"As a deubiquitinase, USP39 specifically interacts with the glycolytic enzyme PGK1 (validated by co-immunoprecipitation coupled with mass spectrometry), stabilizing PGK1 protein levels via deubiquitination [ xref ]."

sparser
"Phosphoglycerate kinase 1 (PGK1), the first ATP-generating enzyme in the glycolytic pathway, has been reported to activate the PI3K/AKT pathway and was chosen for further binding validation by investigating whether endogenous USP39 and PGK1 could interact with each other."