Ubiquitin Specific Peptidase 4 Proteine (USP4)

Human Ubiquitin Specific Peptidase 4 (USP4) Interaktionspartner

1. Data showed significantly increased expression of USP4 in cancer tissues compared to that in para-carcinoma tissues.

2. 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.

3. These results identify USP4 as a novel regulator of Dvl in Wnt/beta-catenin signal and show its involvement in Wnt3a-induced osteoblast differentiation

4. 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.

5. USP4 inhibits p53 and NF-kappaB through deubiquitinating and stabilizing HDAC2

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

7. 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.

8. 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.

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

10. USP4 cooperates with CtIP in DNA double-strand break end resection.

11. 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.

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

13. USP4 requires its N-terminal DUSP-Ubl domain to achieve full catalytic turnover by promoting ubiquitin exchange.

14. USP4 and IL-17 mRNA, but not RORgammat mRNA, were significantly elevated in CD4(+) T cells from patients with rheumatic heart disease

15. USP4 overexpression is associated with hepatocellular carcinoma.

16. Authors identified USP4 as a new positive regulator for RIG-I that acts through deubiquitinating K48-linked ubiquitin chains and stabilizing RIG-I.

17. 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.

18. the interaction with USP4 may regulate the structure and function of the proteasome or the turnover of specific proteasomal substrates.

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

20. Results uncover USP4 as an important determinant for crosstalk between TGF-beta/TGF-beta type I receptor and AKT signalling pathways.

Mouse (Murine) Ubiquitin Specific Peptidase 4 (USP4) Interaktionspartner

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 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.

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 type I receptor and AKT signalling pathways.

5. USP4 interacts directly with and deubiquitinates ARF-BP1, leading to the stabilization of ARF-BP1 and subsequent reduction of p53 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.