IndraLab

Statements


9 | 4 20

sparser
"In gastric cancer, overexpression of PLAGL2 facilitates the proliferation and migration of gastric cancer cells and contributes to the process of epithelial–mesenchymal transition (EMT) via the USP37-Snail1 axis [ xref ]."

reach
"USP37 directly binds, deubiquitinates, and stabilizes SNAI1."

No evidence text available

No evidence text available

No evidence text available

No evidence text available

No evidence text available

No evidence text available

No evidence text available

sparser
"Pleomorphic adenoma gene like-2 (PLAGL2), a zinc finger plag transcription factor, activates the transcription of USP37, a DUB, which subsequently interacts with Snail1 to facilitate its deubiquitination."

No evidence text available

No evidence text available

sparser
"Deubiquitinase USP37 Interacts With Snail."

sparser
"We further examined the interaction between Snail and USP37 by performing co-IP assays."

sparser
"The Western blot assays showed that GST-Snail efficiently co-eluted with USP37, indicating a direct interaction between Snail and USP37 ( xref )."

sparser
"USP37 directly binds, deubiquitinates, and stabilizes SNAI1."

sparser
"We further investigated the interaction between USP37 and Snail1."

sparser
"Also, the reciprocal co-immunoprecipitation analysis demonstrated that endogenous USP37 and Snail1 bound to each other in SGC7901 and AGS cells (Figure xref F)."

sparser
"To map the binding protein domains for Snail1 interacting with USP37, we constructed a series of HA-Snail1 truncations and found that the serine-rich domain (SRD) within Snail1 is required for its interaction with USP37 (Figure xref G-H)."

sparser
"Given that the SRD domain is essential for the interaction between USP37 and Snail1, we evaluated its effect on Snail1 ubiquitination in HEK293T cells."

sparser
"Therefore, the SRD domain is also crucial for USP37-mediated Snail1 deubiquitination and the interaction between USP37 and Snail1."

sparser
"To explore whether the interaction between Snail1 and USP37 requires Snail1 phosphorylation, we utilized CIP to remove phosphate groups from the substrate proteins."

sparser
"Strikingly, Co-IP experiments showed that the interaction between USP37 and Snail1 was strongly impeded by CIP intervention (Figure xref A)."

sparser
"Since GSK-3β is the major kinase involved in Snail1 phosphorylation in the SRD region, the GSK-3β inhibitor LiCl was used to assess GSK-3β inhibition in the interaction of USP37 and Snail1."

sparser
"As shown in Figure xref B, LiCl treatment also significantly disrupted the USP37 and Snail1 interaction."

sparser
"The specific GSK-3β siRNAs were further used to investigate the role of GSK-3β in the interaction between Snail1 and the USP37 protein."

sparser
"Co-IP results showed that GSK-3β siRNAs diminished approximately 60% of the interaction of USP37 and Snail1 (Figure xref D)."

sparser
"Removal of phosphate groups from SNAI1 with a dephosphorylase enzyme reduces the interaction between USP37 and SNAI1; therefore, phosphorylation is required for their interaction."
| PMC

reach
"Of these three DUBs, USP37 binds SNAI1 most strongly and plays a major role in stabilizing SNAI1 and thereby promoting cancer cell migration, E cadherin downregulation, and vimentin upregulation."
| PMC

reach
"They transfected plasmids encoding 79 DUBs into 293 T cells expressing Flag-SNAI1 and found that USP37 predominantly interacts and stabilizes SNAI1 by causing its deubiquitination."
| PMC

reach
"Removal of phosphate groups from SNAI1 with a dephosphorylase enzyme reduces the interaction between USP37 and SNAI1; therefore, phosphorylation is required for their interaction."
| PMC

sparser
"Overexpression of USP37 in SGC7901-shRNA cells restores Snail1 protein levels, which shows that the USP37-Snail1 axis plays a vital role in PLAGL2-mediated Snail1 stabilization."

sparser
"However, in cells with high expression of USP37, phosphorylated Snail1 promotes the mutual binding of USP37 and Snail1, and the ability of USP37 to bind to phosphorylated Snail1 is significantly enhanced."