Ubiquitin Specific Peptidase 4 Proteins (USP4)

Human Ubiquitin Specific Peptidase 4 (USP4) interaction partners

1. These results identify USP4 as a novel regulator of Dvl (show DVL2 Proteins) in Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signal and show its involvement in Wnt3a (show WNT3A Proteins)-induced osteoblast differentiation

2. Data suggest that ubiquitin specific protease 4 (USP4) interacts with interferon regulatory factor 8 (IRF8 (show IRF8 Proteins)) and, by its Lys48-specific deubiquitinase/endopeptidase activity, stabilizes IRF8 (show IRF8 Proteins) protein levels in regulatory T-lymphocytes; USP4 and IRF8 (show IRF8 Proteins) are also expressed in helper T-lymphocytes.

3. USP4 inhibits p53 (show TP53 Proteins) and NF-kappaB (show NFKB1 Proteins) through deubiquitinating and stabilizing HDAC2 (show HDAC2 Proteins)

4. ubiquitin-specific protease 4 (USP4) is a binding partner of RNPS1 (show RNPS1 Proteins).

5. Data indicate that programmed cell death 4 (PDCD4 (show PDCD4 Proteins)) was identified to be a target of ubiquitin-specific protease 4 (USP4), which plays a role as a tumor suppressor.

6. Ubiquitin-specific protease 4 (USP4), recently identified as a beta (show SUCLA2 Proteins)-catenin (show CTNNB1 Proteins)-specific deubiquitinylating enzyme, was highly expressed in PC14PE6/LvBr4 cells and involved in the increased stability of beta-catenin (show CTNNB1 Proteins) protein.

7. USP4 knockdown in HCT116, a colon cancer cell line, reduced invasion and migration activity.

8. USP4 cooperates with CtIP (show RBBP8 Proteins) in DNA double-strand break end resection.

9. 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.

10. findings thus identify USP4 as a novel DNA repair regulator and invoke a model in which ubiquitin adducts regulate USP enzyme interactions and functions.

Mouse (Murine) Ubiquitin Specific Peptidase 4 (USP4) interaction partners

1. In this study, we identified ubiquitin-specific protease 4 (USP4), one of deubiquitinating enzymes, as a suppressor of MRFs by demonstrating that a knockdown of USP4 enhances myogenesis by controlling MyoD (show MYOD1 Proteins) and the level of myogenesis marker proteins in C2C12 cells... we propose that USP4 is a key player in myogenic differentiation; it controls myogenic regulatory factors in a catalytic-independent manner

2. The authors demonstrated that ubiquitin-specific protease (USP) 4 strongly induces activin/BMP signaling by removing the inhibitory monoubiquitination from SMAD4 (show SMAD4 Proteins).

3. USP4 plays an essential role in negative regulation of the TLR/IL-1R signaling-mediated innate immune response

4. Results uncover USP4 as an important determinant for crosstalk between TGF-beta/TGF-beta (show TGFB1 Proteins) type I receptor (show TGFBR1 Proteins) and AKT (show AKT1 Proteins) signalling pathways.

5. USP4 interacts directly with and deubiquitinates ARF-BP1, leading to the stabilization of ARF-BP1 and subsequent reduction of p53 (show TP53 Proteins) levels.

6. the existence of a nuclear export signal ((133)VEVYLLELKL(142)) in Usp4;Usp4 is thus the first oncogenic deubiquitylating enzyme reported to have nucleocytoplasmic shuttling properties.