-
Data showed significantly increased expression of USP4 in cancer tissues compared to that in para-carcinoma tissues.
-
The data indicate that USP4 interacts with and deubiquitinates IRF4, and also stabilizes IRF4 protein and promotes IRF4 function to facilitate IL-4 expression in Th2 cells, which may be related to the pathological process of rheumatic heart disease.
-
These results identify USP4 as a novel regulator of Dvl in Wnt/beta-catenin signal and show its involvement in Wnt3a-induced osteoblast differentiation
-
Data suggest that ubiquitin specific protease 4 (USP4) interacts with interferon regulatory factor 8 (IRF8) and, by its Lys48-specific deubiquitinase/endopeptidase activity, stabilizes IRF8 protein levels in regulatory T-lymphocytes; USP4 and IRF8 are also expressed in helper T-lymphocytes.
-
USP4 inhibits p53 and NF-kappaB through deubiquitinating and stabilizing HDAC2
-
ubiquitin-specific protease 4 (USP4) is a binding partner of RNPS1.
-
Data indicate that programmed cell death 4 (PDCD4) was identified to be a target of ubiquitin-specific protease 4 (USP4), which plays a role as a tumor suppressor.
-
Ubiquitin-specific protease 4 (USP4), recently identified as a beta-catenin-specific deubiquitinylating enzyme, was highly expressed in PC14PE6/LvBr4 cells and involved in the increased stability of beta-catenin protein.
-
USP4 knockdown in HCT116, a colon cancer cell line, reduced invasion and migration activity.
-
USP4 cooperates with CtIP in DNA double-strand break end resection.
-
Results demonstrate that aberrant expression of USP4 contributes to the development and progression of colorectal cancer and reveal a critical mechanism underlying USP4-mediated oncogenic activity.
-
findings thus identify USP4 as a novel DNA repair regulator and invoke a model in which ubiquitin adducts regulate USP enzyme interactions and functions.
-
USP4 requires its N-terminal DUSP-Ubl domain to achieve full catalytic turnover by promoting ubiquitin exchange.
-
USP4 and IL-17 mRNA, but not RORgammat mRNA, were significantly elevated in CD4(+) T cells from patients with rheumatic heart disease
-
USP4 overexpression is associated with hepatocellular carcinoma.
-
Authors identified USP4 as a new positive regulator for RIG-I that acts through deubiquitinating K48-linked ubiquitin chains and stabilizing RIG-I.
-
Data suggest that USP4 down-regulates RIP1 (receptor-interacting serine-threonine kinase 1)-mediated TNFalpha (tumor necrosis factor-alpha) activation and promotes TNFalpha-induced apoptosis via deubiquitination of RIP1 in head/neck carcinoma.
-
the interaction with USP4 may regulate the structure and function of the proteasome or the turnover of specific proteasomal substrates.
-
USP4 plays an essential role in negative regulation of the TLR/IL-1R signaling-mediated innate immune response
-
Results uncover USP4 as an important determinant for crosstalk between TGF-beta/TGF-beta type I receptor and AKT signalling pathways.