HSV ICP0 recruits USP7 to modulate TLR-mediated innate response

Daubeuf, Sandrine; Singh, Divyendu; Tan, Yaohong; Liu, Hongiu; Federoff, Howard J.; Bowers, William J.; Tolba, Khaled A.

doi:10.1182/blood-2008-07-168203

Cited by 127 publications

(135 citation statements)

References 64 publications

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“…HBX41,108 treatment increased p65 ubiquitination in both untreated and TNFα treated cells (Fig. 5D) but did not alter NF-κB essential modulator (NEMO) ubiquitination in line with previous reports (17) (Fig. S7).…”

Section: Resultssupporting

confidence: 79%

“…The proinflammatory nature of many of the transcriptional targets of NF-κB including cytokines and chemokines and their ability to inflict host damage may necessitate such a DNA-binding-induced degradation default. Previous studies have demonstrated that the Herpes Simplex Virus protein ICP0 can mediate the cytoplasmic translocation of USP7 where it interacts with NEMO and TRAF6 (17). Thus, ICP0, by altering USP7 localization, may transform USP7 from a positive to a negative regulator of NF-κB activity.…”

Section: Discussionmentioning

confidence: 99%

“…Of the deubiquitinases studied to date, Ubiquitin Specific Protease-7 (USP7) or herpesvirus-associated ubiquitin-specific protease (HAUSP) has the clearest biological role as a regulator of transcription (15). 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).…”

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confidence: 99%

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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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Section: Resultssupporting

confidence: 79%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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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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“…For this purpose, we first determined whether USP7-promoted PHF8 stabilization is dependent on the enzymatic activity of USP7. To this end, we generated 2 stable MCF-7 cell lines with Dox-inducible expression of wildtype USP7 (USP7/WT) and a catalytically inactive mutant of USP7 (USP7/C223S) (20), respectively. Western blotting analysis els of ubiquitinated PHF8 species ( Figure 3E).…”

Section: Resultsmentioning

confidence: 99%

“…Of the deubiquitinases studied to date, ubiquitin-specific protease 7 (USP7), also known as herpes virus-associated ubiquitin-specific protease (HAUSP), as it was originally identified as a herpes simplex virus type 1 Vmw110-interacting protein (19), is reported to stabilize a number of proteins thus involved in multiple cellular processes, including immune responses (20), viral replication/infection (21), mitosis progression (22), and DNA repair (23,24). It is also found that USP7 forms a protein complex with guanosine 5′-monophosphate synthetase to catalyze the removal of H2B lysine 120 (H2BK120)…”

Section: Introductionmentioning

confidence: 99%

Stabilization of histone demethylase PHF8 by USP7 promotes breast carcinogenesis

Wang¹,

Ma²,

Song³

et al. 2016

Journal of Clinical Investigation

167

172

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Targeting ubiquitin specific protease 7 in cancer: A deubiquitinase with great prospects

Khusbu

Chen

2018

Cell Biochemistry & Function

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Deubiquitinase (DUB)-mediated cleavage of ubiquitin chain balances ubiquitination and deubiquitination for determining protein fate. USP7 is one of the best characterized DUBs and functionally important. Numerous proteins have been identified as potential substrates and binding partners of USP7; those play crucial roles in diverse array of cellular and biological processes including tumour suppression, cell cycle, DNA repair, chromatin remodelling, and epigenetic regulation. This review aims at summarizing the current knowledge of this wide association of USP7 with many cellular processes that enlightens the possibility of abnormal USP7 activity in promoting oncogenesis and the importance of identification of specific inhibitors.

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HSV ICP0 recruits USP7 to modulate TLR-mediated innate response

Cited by 127 publications

References 64 publications

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

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

Stabilization of histone demethylase PHF8 by USP7 promotes breast carcinogenesis

Targeting ubiquitin specific protease 7 in cancer: A deubiquitinase with great prospects

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