USP7, a Ubiquitin-Specific Protease, Interacts with Ataxin-1, the SCA1 Gene Product

Hong, Sunghoi; Kim, Sung Jo; Ka, Sojeong; Choi, In Keun; Kang, Seongman

doi:10.1006/mcne.2002.1103

Cited by 61 publications

(28 citation statements)

References 20 publications

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“…Moreover, in Drosophila, RNA increases toxicity of the ataxin-3 polyQ repeat (Li et al, 2008). Lastly, HAUSP has been shown to bind ataxin-1 and to lose this interaction with the polyQ variant (Hong et al, 2002). Although these are presently circumstantial observations, we raise the possibility that these neuronal aggregates may represent the nucleolus-associated aggregates described here.…”

Section: Nucleolar Aggregates L Latonen Et Almentioning

confidence: 61%

Proteasome inhibitors induce nucleolar aggregation of proteasome target proteins and polyadenylated RNA by altering ubiquitin availability

et al. 2010

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Section: Nucleolar Aggregates L Latonen Et Almentioning

confidence: 61%

Proteasome inhibitors induce nucleolar aggregation of proteasome target proteins and polyadenylated RNA by altering ubiquitin availability

et al. 2010

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“…22,23 Cells were fixed in 3.7% formaldehyde for 15 min and quenched for 10 min in PBS containing 50 mM NH 4 Cl. Subsequently, the cells were permeabilized for 10 min in PBS containing 0.1% Triton X-100.…”

Section: Methodsmentioning

confidence: 99%

Depletion of PKD1 by an antisense oligodeoxynucleotide induces premature G1/S-phase transition

et al. 2004

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Autosomal dominant polycystic kidney disease (ADPKD) is characterized by the growth of epithelial cells and the influx of cyst fluid. The 14-kb mRNA of the polycystic kidney disease gene, PKD1, encodes the polycystin-1 protein, whose function remains unknown. In this study, we observed that polycystin-1 localized in epithelial cell -cell contacts of 293 cells. We found, by bromodeoxyuridine (BrdU) incorporation experiments and Western blot analysis of S-phase-specific cyclins, that the depletion of polycystin-1 led to an increased cell proliferation rate and caused a premature G1/S-phase transition. In addition, we showed that the depletion of polycystin-1 reduced the amount of p53 in 293 cells irradiated by UV light, suggesting that polycystin-1 acts as a regulator of G1 checkpoint, which controls entry into the S phase and prevents the replication of damaged DNA. Our results might provide an insight into the formation and progression of ADPKD cysts.

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“…Originally identified as a herpes simplex virus type 1 (HSV1) Vmw110 interacting protein (16), USP7 also interacts with the Epstein-Barr nuclear antigen 1 (EBNA1) protein and HSV1 IPC0, which can induce the nuclear export of USP7 following infection (17). Identified targets of USP7 deubiquitinase activity include the tumor suppressor protein p53 (18) and its regulator murine double minute (mdm2) (19), PTEN (20), INK4a (21), TSPYL5 (22), Ataxin-1 (23), and the transcription factors FOXO4 (24) and REST (25). The effects of USP7 deubiquitinase activity on these substrates includes enhanced stability as well as altered subcellular localization.…”

mentioning

confidence: 99%

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription

Colleran

Collins

O’Carroll

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

132

119

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NF-κB is the master regulator of the immune response and is responsible for the transcription of hundreds of genes controlling inflammation and immunity. Activation of NF-κB occurs in the cytoplasm through the kinase activity of the IκB kinase complex, which leads to translocation of NF-κB to the nucleus. Once in the nucleus, NF-κB transcriptional activity is regulated by DNA binding-dependent ubiquitin-mediated proteasomal degradation. We have identified the deubiquitinase Ubiquitin Specific Protease-7 (USP7) as a regulator of NF-κB transcriptional activity. USP7 deubiquitination of NF-κB leads to increased transcription. Loss of USP7 activity results in increased ubiquitination of NF-κB, leading to reduced promoter occupancy and reduced expression of target genes in response to Toll-like-and TNF-receptor activation. These findings reveal a unique mechanism controlling NF-κB activity and demonstrate that the deubiquitination of NF-κB by USP7 is critical for target gene transcription.

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USP7, a Ubiquitin-Specific Protease, Interacts with Ataxin-1, the SCA1 Gene Product

Cited by 61 publications

References 20 publications

Proteasome inhibitors induce nucleolar aggregation of proteasome target proteins and polyadenylated RNA by altering ubiquitin availability

Proteasome inhibitors induce nucleolar aggregation of proteasome target proteins and polyadenylated RNA by altering ubiquitin availability

Depletion of PKD1 by an antisense oligodeoxynucleotide induces premature G1/S-phase transition

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription

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