MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-κB signaling

Liang, Jian; Saad, Yasser; Lei, Tianhua; Wang, Jing; Qi, Dawei; Yang, Qinglin; Kolattukudy, Pappachan E.; Fu, Mingui

doi:10.1084/jem.20092641

Cited by 270 publications

(319 citation statements)

References 38 publications

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“…The DUB group of isopeptidases has recently expanded after the description of a new domain in the MCPIP1 protein, which exhibits deubiquitylating activity (Liang et al, 2010). The finding of this novel domain with DUB activity points to the existence of a sixth family of DUBs in the human genome, which according to our bioinformatic analysis, should be composed of at least seven members (Figure 1 and Supplementary Table 1).…”

Section: The Large and Complex Group Of Dubsmentioning

confidence: 84%

“…Conversely, ubiquitin removal is catalyzed by DUBs, which specifically cleave the isopeptide bond between the e-amino group of lysine side chains of target proteins and the Cterminal group of ubiquitin, or the peptidic bond between the a-amino group of the target protein and the Cterminal group of ubiquitin (Wilkinson, 1997). The human genome encodes at least 98 DUBs subdivided into 6 families based on sequence and structural similarity: ubiquitin-specific proteases (USPs), ubiquitin carboxy-terminal hydrolases (UCHs), ovarian-tumor proteases (OTUs), Machado-Joseph disease protein domain proteases, JAMM/MPN domain-associated metallopeptidases (JAMMs) and the recently discovered monocyte chemotactic protein-induced protein (MCPIP) family (Reyes-Turcu et al, 2009;Komander et al, 2009a;Liang et al, 2010). All of them are cysteine proteases with the exception of JAMMs, which belong to the catalytic class of metalloproteases (Figure 1, Supplementary Table 1 and http://degradome.uniovi.es).…”

Section: The Large and Complex Group Of Dubsmentioning

confidence: 99%

“…The N-terminal conserved region and CCCH zinc fingers are critical for MCPIP1 activity. Moreover, the catalytic domain contains the Cys and Asp boxes characteristic of cysteine proteases, but lacks the His box that is likely located outside the N-terminal conserved region (Liang et al, 2010).…”

Section: The Large and Complex Group Of Dubsmentioning

confidence: 99%

“…USP4 also has a critical role in the downregulation of TNFa-induced NF-kB activation through deubiquitylation of TGF-b-activated kinase 1 (Fan et al, 2011). Finally, MCPIP1 negatively regulates c-Jun N-terminal kinase and NF-kB activity through deubiquitylation of TRAF2, TRAF3 and TRAF6, thus having an essential role in inflammatory signaling (Liang et al, 2010).…”

Section: Signaling Pathwaysmentioning

confidence: 99%

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Deubiquitinases in cancer: new functions and therapeutic options

et al. 2011

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Deubiquitinases (DUBs) have fundamental roles in the ubiquitin system through their ability to specifically deconjugate ubiquitin from targeted proteins. The human genome encodes at least 98 DUBs, which can be grouped into 6 families, reflecting the need for specificity in their function. The activity of these enzymes affects the turnover rate, activation, recycling and localization of multiple proteins, which in turn is essential for cell homeostasis, protein stability and a wide range of signaling pathways. Consistent with this, altered DUB function has been related to several diseases, including cancer. Thus, multiple DUBs have been classified as oncogenes or tumor suppressors because of their regulatory functions on the activity of other proteins involved in tumor development. Therefore, recent studies have focused on pharmacological intervention on DUB activity as a rationale to search for novel anticancer drugs. This strategy may benefit from our current knowledge of the physiological regulatory mechanisms of these enzymes and the fact that growth of several tumors depends on the normal activity of certain DUBs. Further understanding of these processes may provide answers to multiple remaining questions on DUB functions and lead to the development of DUB-targeting strategies to expand the repertoire of molecular therapies against cancer.

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Section: The Large and Complex Group Of Dubsmentioning

confidence: 84%

Section: The Large and Complex Group Of Dubsmentioning

confidence: 99%

Section: The Large and Complex Group Of Dubsmentioning

confidence: 99%

Section: Signaling Pathwaysmentioning

confidence: 99%

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Deubiquitinases in cancer: new functions and therapeutic options

et al. 2011

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“…The mammalian genome encodes nearly 100 putative DUBs. DUBs are classified into 6 subfamilies according to the structure of their catalytic domain: Ub‐specific proteases (USPs), Ub C‐terminal hydrolases (UCHs), ovarian tumour‐like proteases (OTUs), JAB1/MPN/Mov34 metalloenzymes (JAMMs), Machado‐Jakob disease (MJD) proteases and a recently identified monocyte chemotactic protein‐induced protein (MCPIP) family 16, 26, 27, 28. This family of DUBs is activated depending on their specificity for the type of Ub chain conjugation attached to the substrate 28.…”

Section: Deubiquitylation Enzymesmentioning

confidence: 99%

The role of K63‐linked polyubiquitination in cardiac hypertrophy

Ponnusamy

Xin

et al. 2018

J Cellular Molecular Medi

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Ubiquitination, also known as ubiquitylation, is a vital post‐translational modification of proteins that play a crucial role in the multiple biological processes including cell growth, proliferation and apoptosis. K63‐linked ubiquitination is one of the vital post‐translational modifications of proteins that are involved in the activation of protein kinases and protein trafficking during cell survival and proliferation. It also contributes to the development of various disorders including cancer, neurodegeneration and cardiac hypertrophy. In this review, we summarize the role of K63‐linked ubiquitination signalling in protein kinase activation and its implications in cardiac hypertrophy. We have also provided our perspectives on therapeutically targeting K63‐linked ubiquitination in downstream effector molecules of growth factor receptors for the treatment of cardiac hypertrophy.

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The Functional Deubiquitinating Enzymes in Control of Innate Antiviral Immunity

Zong

Zhang

et al. 2020

Advanced Science

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Innate antiviral immunity is the first line of host defense against invading viral pathogens. Immunity activation primarily relies on the recognition of pathogen‐associated molecular patterns (PAMPs) by pattern recognition receptors (PRRs). Viral proteins or nucleic acids mainly engage three classes of PRRs: Toll‐like receptors (TLRs), retinoic acid‐inducible gene I (RIG‐I)‐like receptors (RLRs), and DNA sensor cyclic GMP‐AMP (cGAMP) synthase (cGAS). These receptors initiate a series of signaling cascades that lead to the production of proinflammatory cytokines and type I interferon (IFN‐I) in response to viral infection. This system requires precise regulation to avoid aberrant activation. Emerging evidence has unveiled the crucial roles that the ubiquitin system, especially deubiquitinating enzymes (DUBs), play in controlling immune responses. In this review, an overview of the most current findings on the function of DUBs in the innate antiviral immune pathways is provided. Insights into the role of viral DUBs in counteracting host immune responses are also provided. Furthermore, the prospects and challenges of utilizing DUBs as therapeutic targets for infectious diseases are discussed.

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MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-κB signaling

Abstract: A previously unappreciated deubiquitinase activity of MCP-induced protein 1 contributes to its role in dampening inflammatory signaling.

Cited by 270 publications

References 38 publications

Deubiquitinases in cancer: new functions and therapeutic options

Deubiquitinases in cancer: new functions and therapeutic options

The role of K63‐linked polyubiquitination in cardiac hypertrophy

The Functional Deubiquitinating Enzymes in Control of Innate Antiviral Immunity

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