IndraLab

Statements


4 | 2 9

sparser
"USP48 interacts with Gli1 through its C-terminal DUSP domain to remove ubiquitin moiety from Gli1."
| PMC

sparser
"USP48 specifically interacts with Gli1 to remove ubiquitin and regulate the Hedgehog signaling pathway, thereby promoting glioblastoma tumorigenesis xref ."

sparser
"In human glioblastoma, USP48 and Gli1 expression levels were positively correlated, and high USP48 expression levels correlated with higher grades of glioma malignancy [ xref ], suggesting that the USP48-Gli1 regulatory axis is critical for glioma cell proliferation and glioblastoma tumorigenesis."
| PMC

sparser
"Additionally, active HH signaling induces USP48 expression via a positive feedback loop by GLI1 binding to the USP48 promoter ( xref )."

reach
"Mechanistically, USP48 interacts with Gli1 and cleaves its ubiquitin off directly."

reach
"USP8 prevents SMO ubiquitylation and increases HH signaling activity by promoting SHH-induced cell surface accumulation of SMO (205, 242), whereas USP48 interacts with GLI1 in the nucleus and thereby protects GLI1 from proteasome-dependent degradation."

sparser
"Zhou and colleagues sustained a positive feedback loop by which HH signaling activates USP48 through the binding of GLI1 to Usp48 promoter."

sparser
"This evidence underlies the relevance of USP48-GLI1 regulatory axis for glioma cell proliferation and glioblastoma tumorigenesis [ xref ]."

sparser
"The deubiquitinase USP48 is able to interact directly with GLI1, cleaving off its ubiquitin and thus enhancing its lifetime. xref In GBM cells, knockdown of USP48 inhibits cell proliferation and expression of GLI1’s downstream targets, leading to repressed tumorigenesis."

sparser
"Depletion of USP48 inhibits glioma cell viability and tumor generation by partially stabilizing Gli1, which incidates a critical role of the USP48Gli1 axis in glioblastoma tumorigenesis ( xref ) ( xref )."

sparser
"USP8 prevents SMO ubiquitylation and increases HH signaling activity by promoting SHH-induced cell surface accumulation of SMO ( xref , xref ), whereas USP48 interacts with GLI1 in the nucleus and thereby protects GLI1 from proteasome-dependent degradation."