The Poxvirus p28 Virulence Factor Is an E3 Ubiquitin Ligase

Huang, Jianing; Huang, Qi; Zhou, Xiulan; Shen, Mary; Yen, Ann; Yu, Shichao; Dong, Guoqiang; Qu, Kun; Huang, Peiyong; Anderson, Emily M.; Daniel-Issakani, Sarkiz; Buller, R. Mark; Payan, Donald G.; Lu, Henry

doi:10.1074/jbc.m410583200

Cited by 67 publications

(62 citation statements)

References 32 publications

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“…Similarly, the RING-finger proteins MBP-IAP2, IE2, and PE38 of Bombyx mori nucleopolyhedrovirus (BmNPV) are able to reconstitute ubiquitination activity in vitro and their activity is dependent on their RING-finger motif [110]. Interestingly, Huang et al [111] demonstrated that the p28 proteins encoded by the ectromelia virus and the variola virus possess E3 ubiquitin ligase activity in biochemical assays as well as in cultured mammalian cells. Point mutations disrupting the RING-finger domain of p28 completely abolish its E3 ligase activity.…”

Section: Pathogen-derived Proteins Act As E3 Ligases In Host Cellsmentioning

confidence: 99%

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

et al. 2006

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Post-translational modification is central to protein stability and to the modulation of protein activity. Various types of protein modification, such as phosphorylation, methylation, acetylation, myristoylation, glycosylation, and ubiquitination, have been reported. Among them, ubiquitination distinguishes itself from others in that most of the ubiquitinated proteins are targeted to the 26S proteasome for degradation. The ubiquitin/26S proteasome system constitutes the major protein degradation pathway in the cell. In recent years, the importance of the ubiquitination machinery in the control of numerous eukaryotic cellular functions has been increasingly appreciated. Increasing number of E3 ubiquitin ligases and their substrates, including a variety of essential cellular regulators have been identified. Studies in the past several years have revealed that the ubiquitination system is important for a broad range of plant developmental processes and responses to abiotic and biotic stresses. This review discusses recent advances in the functional analysis of ubiquitination-associated proteins from plants and pathogens that play important roles in plant-microbe interactions.

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Section: Pathogen-derived Proteins Act As E3 Ligases In Host Cellsmentioning

confidence: 99%

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

et al. 2006

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“…It remains unclear whether HCV core induces proteosome-mediated core11 degradation. However, there is growing evidence that proteosome activity may be directed by a diverse range of viral proteins as part of an efficient viral propagation strategy (61)(62)(63)(64)(65)(66)(67). Indeed, it was recently reported that the core protein of HBV stimulates the proteasome-mediated degradation of the HBV X protein (HBX), when the HBV viral proteins, which are transcriptionally transactivated by the X protein, reach a sufficiently high levels for viral replication (68)(69)(70)(71)(72).…”

Section: Biochemical Properties Of Core11 Proteinsmentioning

confidence: 99%

The HCV ARFP/F/core+1 protein: Production and functional analysis of an unconventional viral product

Vassilaki

Mavromara

2009

IUBMB Life

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Hepatitis C virus (HCV) is an enveloped positive‐strand RNA virus of the Flaviviridae family. It has a genome of about 9,600 nucleotides encoding a large polyprotein (about 3,000 amino acids) that is processed by cellular and viral proteases into at least 10 structural and nonstructural viral proteins. A novel HCV protein has also been identified by our laboratory and others. This protein—known as ARFP (alternative reading frame protein), F (for frameshift) or core+1 (to indicate the position) protein ‐ is synthesized by an open reading frame overlapping the core gene at nucleotide +1 (core+1 ORF). However, almost 10 years after its discovery, we still know little of the biological role of the ARFP/F/core+1 protein. Abolishing core+1 protein production has no affect on HCV replication in cell culture or uPA‐SCID mice, suggesting that core+1 protein is probably not important for the HCV reproductive cycle. However, the detection of specific anti‐core+1 antibodies and T‐cell responses in HCV‐infected patients, as reported by many independent laboratories, provides strong evidence that this protein is produced in vivo. Furthermore, analyses of the HCV sequences isolated from patients with hepatocellular carcinoma and in vitro studies have provided strong preliminary evidence to suggest that core+1 protein plays a role in advanced liver disease and liver cancer. The available in vitro data also suggest that certain core function proteins may depend on production of the core+1 protein. We describe here the discovery of the various forms of the core+1 protein and what is currently known about the mechanisms of their production and their biochemical and functional properties. We also provide a detailed summary of the results of patient‐based research. © 2009 IUBMB IUBMB Life, 61(7): 739–752, 2009

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“…The sequence of oligonucleotides 16615 (with 5Ј-FAM) and 13657 is 5Ј-CUAGCACGAACU UGUUUACCCUCCC-3Ј. FLAG-and His-tagged wild-type Ub as well as various K to R mutants of Ub were expressed and purified from Escherichia coli as described by Huang et al (41).…”

Section: Reagentsmentioning

confidence: 99%

A Novel E3 Ubiquitin Ligase TRAC-1 Positively Regulates T Cell Activation

Zhao

Pardo

et al. 2005

The Journal of Immunology

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TRAC-1 (T cell RING (really interesting new gene) protein identified in activation screen) is a novel E3 ubiquitin ligase identified from a retroviral vector-based T cell surface activation marker screen. The C-terminal truncated TRAC-1 specifically inhibited anti-TCR-mediated CD69 up-regulation in Jurkat cells, a human T leukemic cell line. In this study, we show that TRAC-1 is a RING finger ubiquitin E3 ligase with highest expression in lymphoid tissues. Point mutations that disrupt the Zn2+-chelating ability of its amino-terminal RING finger domain abolished TRAC-1’s ligase activity and the dominant inhibitory effect of C-terminal truncated TRAC-1 on TCR stimulation. The results of in vitro biochemical studies indicate that TRAC-1 can stimulate the formation of both K48- and K63-linked polyubiquitin chains and therefore could potentially activate both degradative and regulatory ubiquitin-dependent pathways. Antisense oligonucleotides to TRAC-1 specifically reduced TRAC-1 mRNA levels in Jurkat and primary T cells and inhibited their activation in response to TCR cross-linking. Collectively, these results indicate that the E3 ubiquitin ligase TRAC-1 functions as a positive regulator of T cell activation.

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The Poxvirus p28 Virulence Factor Is an E3 Ubiquitin Ligase

Cited by 67 publications

References 32 publications

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

The HCV ARFP/F/core+1 protein: Production and functional analysis of an unconventional viral product

A Novel E3 Ubiquitin Ligase TRAC-1 Positively Regulates T Cell Activation

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