USP7 deubiquitinase controls HIV-1 production by stabilizing Tat protein

Ali, Amjad; Raja, Rameez; Farooqui, Sabihur Rahman; Ahmad, Shaista; Banerjea, Akhil C.

doi:10.1042/bcj20160304

Cited by 44 publications

(41 citation statements)

References 46 publications

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“…UL35 protein from cytomegalovirus essential for viral replication also interacts with USP7 . USP7 is upregulated in HIV‐1 infected cells resulting in stabilization of Tat protein and eventually increased virus production . Interaction of USP7 with these viral proteins indicates that several viruses partly use deubiquitination process for their successful infection within the host, and future studies may uncover the relationship of USP7 with this virus‐mediated tumorigenesis.…”

Section: Ubiquitin Specific Protease 7 (Usp7)mentioning

confidence: 99%

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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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Section: Ubiquitin Specific Protease 7 (Usp7)mentioning

confidence: 99%

“…44 USP7 is upregulated in HIV-1 infected cells resulting in stabilization of Tat protein and eventually increased virus production. 100 Interaction of USP7…”

Section: Usp7 Regulates the Activity Of Foxo Family Of Transcriptiomentioning

confidence: 99%

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

Khusbu

Chen

2018

Cell Biochemistry & Function

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“…UPS system contains basically three principle components: the proteasome holoenzymes, multiple ubiquitin ligases, and several kind of deubiquitinating enzymes (DUBs) . Many eukaryotic viruses have been recognized in influencing host protein ubiquitination machinery to facilitate their life cycle . Similarly, deubiquitination phenomenon is also exploited by many viruses to accomplish their life cycle and manifest all facets of their pathogenesis .…”

Section: Introductionmentioning

confidence: 99%

“…24 Many eukaryotic viruses have been recognized in influencing host protein ubiquitination machinery to facilitate their life cycle. 5,25 Similarly, deubiquitination phenomenon is also exploited by many viruses to accomplish their life cycle and manifest all facets of their pathogenesis. [26][27][28] In our previous reports, we have established that one of the DUBs, USP7, stabilizes HIV-1 Tat protein through its deubiquitination which in turn leads to enhance viral replication of HIV-1.…”

Section: Introductionmentioning

confidence: 99%

“…[26][27][28] In our previous reports, we have established that one of the DUBs, USP7, stabilizes HIV-1 Tat protein through its deubiquitination which in turn leads to enhance viral replication of HIV-1. 25 Ubiquitin-specific protease 42 (USP42) is a deubiquitinating enzyme (DUB) which is widely expressed in multiple human tissues. 29 USP42 is well-known to target p53 and stabilizes p53 in response to stress.…”

Section: Introductionmentioning

confidence: 99%

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Dengue NS5 modulates expression of miR‐590 to regulate ubiquitin‐specific peptidase 42 in human microglia

2019

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Dengue virus (DENV), a member of Flaviviridae family, has become neurovirulent in humans after rapid geographical expansion. Host proteasomal machinery contains both ubiquitin ligases as well as deubiquitinases (DUBs), known to influence key cellular and biological functions. MicroRNA‐mediated modulations of DUBs in case of DENV infections have not been explored yet. DENV propagation, MiRNA overexpression, miRNA knockdown, transfection, RT‐PCR, luciferase assay, and western blotting have been used in this study to establish the interaction of miR‐590 and USP42. DENV infection in human microglial cells resulted in downregulation of host DUB‐USP42 in a dose‐dependent manner and DENV‐NS5 gene alone was found to be sufficient for this downregulation. miR‐590 was upregulated upon NS5 overexpression in a dose‐dependent manner. Downregulation of USP42 was observed with miR‐590 overexpression. The specificity of this regulation was confirmed by miR‐590 mimic and anti‐miR transfections in microglial cells. miR‐590 overexpression and knockdown affected the expression level of TRAF6 in indirect manner in microglial cells. The luciferase assay demonstrated the direct regulatory interaction between miR‐590 and 3’UTR of USP42. These findings establish that DENV‐NS5 protein can potentially modulate the host deubiquitinase protein USP42 expression via altering cellular miR‐590 levels in human microglial cells.

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Acute Administration of HIV-1 Tat Protein Drives Glutamatergic Alterations in a Rodent Model of HIV-Associated Neurocognitive Disorders

Duffy,

King,

Nepal

et al. 2024

Mol Neurobiol

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HIV-1-associated neurocognitive disorders (HAND) are a major comorbidity of HIV-1 infection, marked by impairment of executive function varying in severity. HAND affects nearly half of people living with HIV (PLWH), with mild forms predominating since the use of anti-retroviral therapies (ART). The HIV-1 transactivator of transcription (Tat) protein is found in the cerebrospinal fluid of patients adherent to ART, and its administration or expression in animals causes cognitive symptoms. Studies of Tat interaction with the N-methyl-D-aspartate receptor (NMDAR) suggest that glutamate toxicity contributes to Tat-induced impairments. To identify changes in regional glutamatergic circuitry underlying cognitive impairment, we injected recombinant Tat86 or saline to medial prefrontal cortex (mPFC) of male Sprague–Dawley rats. Rats were assessed with behavioral tasks that involve intact functioning of mPFC including the novel object recognition (NOR), spatial object recognition (SOR), and temporal order (TO) tasks at 1 and 2 postoperative weeks. Following testing, mPFC tissue was collected and analyzed by RT-PCR. Results showed Tat86 in mPFC-induced impairment in SOR, and upregulation of Grin1 and Grin2a transcripts. To further understand the mechanism of Tat toxicity, we assessed the effects of full-length Tat101 on gene expression in mPFC by RNA sequencing. The results of RNAseq suggest that glutamatergic effects of Tat86 are maintained with Tat101, as Grin2a was upregulated in Tat101-injected tissue, among other differentially expressed genes. Spatial learning and memory impairment and Grin2a upregulation suggest that exposure to Tat protein drives adaptation in mPFC, altering the function of circuitry supporting spatial learning and memory.

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USP7 deubiquitinase controls HIV-1 production by stabilizing Tat protein

Cited by 44 publications

References 46 publications

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

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

Dengue NS5 modulates expression of miR‐590 to regulate ubiquitin‐specific peptidase 42 in human microglia

Acute Administration of HIV-1 Tat Protein Drives Glutamatergic Alterations in a Rodent Model of HIV-Associated Neurocognitive Disorders

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