The <scp>RING</scp> domain of <scp>RING</scp> Finger 11 (<scp>RNF</scp>11) protein binds Ubc13 and inhibits formation of polyubiquitin chains

Budhidarmo, Rhesa; Zhu, Junjie; Middleton, Adam J.; Day, Catherine L.

doi:10.1002/1873-3468.13029

Cited by 8 publications

(8 citation statements)

References 50 publications

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“…Therefore, deamidases may provide a direction for targeted therapy of TRAF6 in tumors. Furthermore, RING Finger protein 11 (RNF11) and the small molecule inhibitor C25-140 downregulate the ubiquitinase activity of TRAF6 by reducing the activity of TRAF6-Ubc13 [99,117].…”

Section: Resultsmentioning

confidence: 99%

The relationship between TRAF6 and tumors

Liu

Tang

et al. 2020

Cancer Cell Int

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Tumor necrosis factor receptor (TNFR)-related factors (TRAFs) are important linker molecules in the tumor necrosis factor superfamily (TNFSF) and the Toll-like/interleukin-1 receptor (TLR/ILR) superfamily. There are seven members: TRAF1-TRAF7, among those members, tumor necrosis factor receptor-associated factor 6 (TRAF6) is upregulated in various tumors, which has been related to tumorigenesis and development. With the in-depth study of the relationship between TRAF6 and different types of tumors, TRAF6 has oncogenic characteristics involved in tumorigenesis, tumor development, invasion, and metastasis through various signaling pathways, therefore, targeting TRAF6 has provided a novel strategy for tumor treatment. This review summarizes and analyzes the role of TRAF6 in tumorigenesis and tumor development in combination with the current research on TRAF6 and tumors.

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Section: Resultsmentioning

confidence: 99%

The relationship between TRAF6 and tumors

Liu

Tang

et al. 2020

Cancer Cell Int

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“…RNF11 is a 154-amino acids protein that contains a canonical RING-H2 finger motif (C3H2C2, 99–140aa) at the carboxyl-terminal end ( Figure 1 ). The RING-H2 domain appears to be a stable folded monomeric domain showing structural similarities with the RING1 domain of RBR E3s [ 12 ]. The full-length protein contains disordered regions, which mainly involving the N-terminal end and the short C-terminal tail following the RING domain (aa 141–154) [ 12 ].…”

Section: Rnf11 a Multifunctional Ring-h2 Ligasementioning

confidence: 99%

“…The RING-H2 domain appears to be a stable folded monomeric domain showing structural similarities with the RING1 domain of RBR E3s [ 12 ]. The full-length protein contains disordered regions, which mainly involving the N-terminal end and the short C-terminal tail following the RING domain (aa 141–154) [ 12 ]. However, the structure of both terminal ends is predicted to be highly influenced by the presence of post-translational modifications and the interaction with binding partners (see below).…”

Section: Rnf11 a Multifunctional Ring-h2 Ligasementioning

confidence: 99%

“…Nevertheless, the presence of a glycine (Gly) instead of the highly conserved serine (Ser) makes the effective functionality of this motif controversial. Accordingly, recent data show that the UIM of RNF11 does not bind ubiquitin in vitro, which leaves open the question whether it acts as a functional ubiquitin binding site in vivo [ 12 ]. Because the non-covalent interaction between E3 enzymes and ubiquitin has clearly been shown to influence the enzymatic activity of almost all the main classes of ligases [ 20 , 21 , 22 , 23 , 24 , 25 , 26 ], clearly defining the ability of RNF11 to bind ubiquitin would provide useful hints regarding its regulatory mechanism.…”

Section: Rnf11 a Multifunctional Ring-h2 Ligasementioning

confidence: 99%

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RNF11 at the Crossroads of Protein Ubiquitination

2020

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RNF11 (Ring Finger Protein 11) is a 154 amino-acid long protein that contains a RING-H2 domain, whose sequence has remained substantially unchanged throughout vertebrate evolution. RNF11 has drawn attention as a modulator of protein degradation by HECT E3 ligases. Indeed, the large number of substrates that are regulated by HECT ligases, such as ITCH, SMURF1/2, WWP1/2, and NEDD4, and their role in turning off the signaling by ubiquitin-mediated degradation, candidates RNF11 as the master regulator of a plethora of signaling pathways. Starting from the analysis of the primary sequence motifs and from the list of RNF11 protein partners, we summarize the evidence implicating RNF11 as an important player in modulating ubiquitin-regulated processes that are involved in transforming growth factor beta (TGF-β), nuclear factor-κB (NF-κB), and Epidermal Growth Factor (EGF) signaling pathways. This connection appears to be particularly significant, since RNF11 is overexpressed in several tumors, even though its role as tumor growth inhibitor or promoter is still controversial. The review highlights the different facets and peculiarities of this unconventional small RING-E3 ligase and its implication in tumorigenesis, invasion, neuroinflammation, and cancer metastasis.

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“…The immune system represents the first defense line raised against pathogen invasion or more generally exogenous danger signals. It is mediated by pathogen-recognition receptors (PRRs) that defend us from invading pathogens by recognizing pathogen-associated molecular patterns (PAMPs) [ 21 , 22 ]. Ubiquitylation and its reversal, deubiquitylation, have been implicated in the development and regulation of the innate and adaptive immune responses.…”

Section: Ubiquitylation In Immune Responsementioning

confidence: 99%

Revisiting Bacterial Ubiquitin Ligase Effectors: Weapons for Host Exploitation

Pisano

Albano

Vecchio

et al. 2018

IJMS

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Protein ubiquitylation plays a central role in eukaryotic cell physiology. It is involved in several regulatory processes, ranging from protein folding or degradation, subcellular localization of proteins, vesicular trafficking and endocytosis to DNA repair, cell cycle, innate immunity, autophagy, and apoptosis. As such, it is reasonable that pathogens have developed a way to exploit such a crucial system to enhance their virulence against the host. Hence, bacteria have evolved a wide range of effectors capable of mimicking the main players of the eukaryotic ubiquitin system, in particular ubiquitin ligases, by interfering with host physiology. Here, we give an overview of this topic and, in particular, we detail and discuss the mechanisms developed by pathogenic bacteria to hijack the host ubiquitination system for their own benefit.

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The RING domain of RING Finger 11 (RNF11) protein binds Ubc13 and inhibits formation of polyubiquitin chains

Cited by 8 publications

References 50 publications

The relationship between TRAF6 and tumors

The relationship between TRAF6 and tumors

RNF11 at the Crossroads of Protein Ubiquitination

Revisiting Bacterial Ubiquitin Ligase Effectors: Weapons for Host Exploitation

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