Early adipogenesis is regulated through USP7-mediated deubiquitination of the histone acetyltransferase TIP60

Gao, Yuan; Koppen, Arjen; Rakhshandehroo, Maryam; Taşdelen, Ismayil; Graaf, Stan F.J. van de; Loosdregt, Jorg van; Beekum, Olivier van; Hamers, Nicole; Leenen, Dik van; Berkers, Celia R.; Berger, Ruud; Holstege, Frank C.P.; Coffer, Paul J.; Brenkman, Arjan B.; Ovaa, Huib; Kalkhoven, Eric

doi:10.1038/ncomms3656

Cited by 58 publications

(50 citation statements)

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“…Through this interaction, ICP0 and USP7 reciprocally modulate each other's stability (13,14). Similar to ICP0 (4-7), USP7 also has a wide range of deubiquitination substrates involved in many critical checkpoints, such as cell cycle regulation, apoptosis, DNA repair, and gene regulation (15)(16)(17)(18). Although the relationships among ICP0, USP7, and their substrates are not yet clear, it is justifiable to postulate that fine-tuning of the levels of these checkpoint proteins can have a pivotal role in the tug-of-war between HSV-1 and the host.…”

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confidence: 99%

Identification of Three Redundant Segments Responsible for Herpes Simplex Virus 1 ICP0 To Fuse with ND10 Nuclear Bodies

Zheng

2015

J Virol

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Infected cell protein 0 (ICP0) of herpes simplex virus 1 (HSV-1) is a key regulator in both lytic and latent infections. In lytic infection, an important early event is the colocalization of ICP0 to nuclear domain 10 (ND10), the discrete nuclear bodies that impose restrictions on viral expression. ICP0 contains an E3 ubiquitin ligase that degrades promyelocytic leukemia protein (PML) and Sp100, two major components of ND10, and disperses ND10 to alleviate repression. We previously reported that the association between ICP0 and ND10 is a dynamic process that includes three steps: adhesion, fusion, and retention. ICP0 residues 245 to 474, defined as ND10 entry signal (ND10-ES), is a region required for the fusion step. Without ND10-ES, ICP0 adheres at the ND10 surface but fails to enter. In the present study, we focus on characterizing ND10-ES. Here we report the following. IMPORTANCE ND10 nuclear bodies are part of the cell-intrinsic antiviral defenses that restrict viral gene expression upon virus infection. As a countermeasure, infected cell protein 0 (ICP0) of herpes simplex virus 1 (HSV-1) localizes to ND10s, degrades the ND10 organizer, and disperses ND10 components in order to alleviate repression. We studied the ICP0-ND10 association to delineate elements important for this dynamic interaction and to understand its role in viral replication and host defense. In this work, we show that ICP0 contains three redundant segments to ensure an effective mergence of ICP0 with ND10 nuclear bodies. This is the first study to systematically investigate ICP0 elements that are important for ICP0-ND10 fusion. Herpes simplex virus 1 (HSV-1) infected cell protein 0 (ICP0) is a multifunctional immediate early protein that plays a key role in both lytic and latent infections. The protein is essential at a low multiplicity of infection (MOI) in cultured cells (1). Its main functions are to counteract cell-intrinsic and innate defenses by targeting saturable cellular restrictive factors and consequently to enhance viral gene expression (1).The 775-amino-acid ICP0 contains a RING (really interesting new gene) type E3 ubiquitin ligase in its second exon (2, 3), which ubiquitinates various cellular proteins for proteasomal degradation. Known ICP0 substrates include promyelocytic leukemia protein (PML) (4), speckled protein Sp100 (4), DNA-dependent protein kinase (DNA-PK) (5), centromeric protein A (CENP-A) (6), and interferon (IFN)-inducible protein 16 (IFI16) (7). Some of these ICP0 substrates are restrictive for HSV-1 infection, inasmuch as small interfering RNA (siRNA) knockdown of PML, Sp100, or IFI16, individually or in combination, enhances viral replication in the absence of ICP0 (8, 9).A second tactic of ICP0 to overcome antiviral defenses is to regulate a diverse array of cell pathways via protein-protein interactions. For example, ICP0 interacts with corepressor of RE1-silencing transcription factor (CoREST). This interaction leads to the dissociation of histone deacetylases (HDACs) 1 and 2 from the REST/CoREST...

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confidence: 99%

Identification of Three Redundant Segments Responsible for Herpes Simplex Virus 1 ICP0 To Fuse with ND10 Nuclear Bodies

Zheng

2015

J Virol

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“…During adipocyte differentiation, cells first undergo growth arrest, re-enter the cell cycle under the influence of differentiation inducers, undergo mitotic clonal expansion and, finally, exit the cell cycle to undergo terminal differentiation (Gao et al, 2013;Tang et al, 2003). During the early phase of adipocyte differentiation, AIMP1 levels increase; the protein then translocates to the nucleus, where it interacts with and inhibits the transcriptional activity of PPARc ( Fig.…”

Section: Discussionmentioning

confidence: 99%

AIMP1/p43 negatively regulates adipogenesis by inhibiting peroxisome proliferator-activated receptor gamma

Kim

Lee

Park

et al. 2014

Journal of Cell Science

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Adipogenesis is known to be controlled by the concerted actions of transcription factors and co-regulators. However, little is known about the mechanism of regulation of the transcription factors that control adipogenesis. In addition, the adipogenic roles of translational factors remain unclear. Here, we show that aminoacyl tRNA synthetaseinteracting multifunctional protein 1 (AIMP1, also known as p43), an auxiliary factor that is associated with a macromolecular tRNA synthetase complex, negatively regulates adipogenesis through a direct interaction with the DNA-binding domain of peroxisome proliferator-activated receptor c (PPARc). We found that AIMP1 expression increases during adipocyte differentiation. Adipogenesis is augmented in AIMP1-deficient cells, as compared with control cells. AIMP1 exhibits high affinity for active PPARc and interacts with the DNA-binding domain of PPARc, thereby inhibiting its transcriptional activity. Thus, AIMP1 appears to function as a novel inhibitor of PPARc that regulates adipocyte differentiation by preventing the transcriptional activation of PPARc.

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“…Ubiquitin specific peptidase 7 (USP7), also known as herpes virus-associated ubiquitin-specific protease (HAUSP), is hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, PTEN, PPARG, and other and thus participate in control of cell growth repression and apoptosis [18][19][20]. There is data that early adipogenesis is regu lated through USP7-mediated deubiquitination of the histone acetyltransferase TIP60 [21]. Transcription factors play an important role in the regulation various metabolic pathways as well as prolife ration and apoptosis.…”

Section: We Have Studied the Effect Of Chromium Disilicide And Titanimentioning

confidence: 99%

Effect of chromium disilicide and titanium nitride nanoparticles on the expression of NAMPT, E2F8, FAS, TBX3, IL13RA2, and UPS7 genes in mouse liver

Minchenko¹,

Yavorovsky²,

Solokha³

et al. 2017

Ukr.Biochem.J.

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Early adipogenesis is regulated through USP7-mediated deubiquitination of the histone acetyltransferase TIP60

Cited by 58 publications

References 59 publications

Identification of Three Redundant Segments Responsible for Herpes Simplex Virus 1 ICP0 To Fuse with ND10 Nuclear Bodies

Identification of Three Redundant Segments Responsible for Herpes Simplex Virus 1 ICP0 To Fuse with ND10 Nuclear Bodies

AIMP1/p43 negatively regulates adipogenesis by inhibiting peroxisome proliferator-activated receptor gamma

Effect of chromium disilicide and titanium nitride nanoparticles on the expression of NAMPT, E2F8, FAS, TBX3, IL13RA2, and UPS7 genes in mouse liver

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