USP7‐TRIM27 axis negatively modulates antiviral type I IFN signaling

Cai, Juan; Chen, Liqun; Peng, Shengnan; Meng, Jun-Ling; Wang, Yan; Zhou, Yu; Qian, Xiaoping; Sun, Xiuyuan; Pang, Xuewen; Zhang, Yu; Zhang, Jun

doi:10.1096/fj.201700473rr

Cited by 45 publications

(41 citation statements)

References 77 publications

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“…Previous studies have shown that TRIM family proteins play important roles in transcriptional control, viral suppression, energy metabolism, development and cellular differentiation, immune response, proliferation, cancer and genome stability, etc Results from others and our group have shown that tripartite motif‐containing 28 (TRIM28) mediates the differentiation of murine embryonic stem cells into cardiomyocytes, angiogenesis, and endothelial inflammatory response . Tripartite motif‐containing 27 (TRIM27) is involved in cell proliferation and transcriptional repression . In this study, we identified that TRIM28 and TRIM27 cooperatively regulate the phenotypic switching through a novel mechanism involving serum response element (SRE) in human VSMCs.…”

Section: Introductionmentioning

confidence: 78%

TRIM28 and TRIM27 are required for expressions of PDGFRβ and contractile phenotypic genes by vascular smooth muscle cells

et al. 2020

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Vascular smooth muscle cells (VSMCs) in the normal arterial media continually express contractile phenotypic markers which are reduced dramatically in response to injury. Tripartite motif-containing proteins are a family of scaffold proteins shown to regulate gene silencing, cell growth, and differentiation. We here investigated the biological role of tripartite motif-containing 28 (TRIM28) and tripartite motif-containing 27 (TRIM27) in VSMCs. We observed that siRNA-mediated knockdown of TRIM28 and TRIM27 inhibited platelet-derived growth factor (PDGF)-induced migration in human VSMCs. Both TRIM28 and TRIM27 can regulate serum response element activity and were required for maintaining the contractile gene expression in human VSMCs. At the same time, TRIM28 and TRIM27 knockdown reduced the expression of PDGF receptor-β (PDGFRβ) and the phosphorylation of its downstream signaling components. Immunoprecipitation showed that TRIM28 formed complexes with TRIM27 through its N-terminal RING-B boxes-Coiled-Coil domain.Furthermore, TRIM28 and TRIM27 were shown to be upregulated and mediate the VSMC contractile marker gene and PDGFRβ expression in differentiating human bone marrow mesenchymal stem cells. In conclusion, we identified that TRIM28 and TRIM27 cooperatively maintain the endogenous expression of PDGFRβ and contractile phenotype of human VSMCs.

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Section: Introductionmentioning

confidence: 78%

TRIM28 and TRIM27 are required for expressions of PDGFRβ and contractile phenotypic genes by vascular smooth muscle cells

et al. 2020

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“…USP7 interacts with TRIM27 and forms the USP7-TRIM27-TBK1 complex, and the interaction between USP7 and TRIM27 can be enhanced after Sendai virus (SeV) infection. When USP7 was overexpressed, TRIM27 can be protected from degradation, which contributed to the ubiquitination and degradation of TBK1, resulting in decreased type I interferons (IFNs) signaling (Cai et al, 2018). As IFNs are a series of signaling proteins which are produced and released by host cells to cope with the presence of pathogens, USP7 can enhance the effects of TRIM27 on TBK1-induced IFN – stimulated response element (ISRE) and IFN-β activation (Zaman et al, 2013).…”

Section: Usp7: One Protein Multiple Rolesmentioning

confidence: 99%

USP7: Novel Drug Target in Cancer Therapy

et al. 2019

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Ubiquitin specific protease 7 (USP7) is one of the deubiquitinating enzymes (DUB) that erases ubiquitin and protects substrate protein from degradation. Full activity of USP7 requires the C-terminal Ub-like domains fold back onto the catalytic domain, allowing the remodeling of the active site to a catalytically competent state by the C-terminal peptide. Until now, numerous proteins have been identified as substrates of USP7, which play a key role in cell cycle, DNA repair, chromatin remodeling, and epigenetic regulation. Aberrant activation or overexpression of USP7 may promote oncogenesis and viral disease, making it a target for therapeutic intervention. Currently, several synthetic small molecules have been identified as inhibitors of USP7, and applied in the treatment of diverse diseases. Hence, USP7 may be a promising therapeutic target for the treatment of cancer.

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“…USP7 was found to bind and remove ubiquitin from TRIM27 allowing for the ubiquitination and degradation of TBK1 (Fig. 6) [159].…”

Section: Negative Regulation Of Host Antiviral Signallingmentioning

confidence: 99%

To TRIM or not to TRIM: the balance of host–virus interactions mediated by the ubiquitin system

Hage

Rajsbaum

2019

Journal of General Virology

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The innate immune system responds rapidly to protect against viral infections, but an overactive response can cause harmful damage. To avoid this, the response is tightly regulated by post-translational modifications (PTMs). The ubiquitin system represents a powerful PTM machinery that allows for the reversible linkage of ubiquitin to activate and deactivate a target's function. A precise enzymatic cascade of ubiquitin-activating, conjugating and ligating enzymes facilitates ubiquitination. Viruses have evolved to take advantage of the ubiquitin pathway either by targeting factors to dampen the antiviral response or by hijacking the system to enhance their replication. The tripartite motif (TRIM) family of E3 ubiquitin ligases has garnered attention as a major contributor to innate immunity. Many TRIM family members limit viruses either indirectly as components in innate immune signalling, or directly by targeting viral proteins for degradation. In spite of this, TRIMs and other ubiquitin ligases can be appropriated by viruses and repurposed as valuable tools in viral replication. This duality of function suggests a new frontier of research for TRIMs and raises new challenges for discerning the subtleties of these pro-viral mechanisms. Here, we review current findings regarding the involvement of TRIMs in host-virus interactions. We examine ongoing developments in the field, including novel roles for unanchored ubiquitin in innate immunity, the direct involvement of ubiquitin ligases in promoting viral replication, recent controversies on the role of ubiquitin and TRIM25 in activation of the pattern recognition receptor RIG-I, and we discuss the implications these studies have on future research directions.

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USP7‐TRIM27 axis negatively modulates antiviral type I IFN signaling

Cited by 45 publications

References 77 publications

TRIM28 and TRIM27 are required for expressions of PDGFRβ and contractile phenotypic genes by vascular smooth muscle cells

TRIM28 and TRIM27 are required for expressions of PDGFRβ and contractile phenotypic genes by vascular smooth muscle cells

USP7: Novel Drug Target in Cancer Therapy

To TRIM or not to TRIM: the balance of host–virus interactions mediated by the ubiquitin system

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