RNF11 is a multifunctional modulator of growth factor receptor signalling and transcriptional regulation

Azmi, Peter; Seth, Arun

doi:10.1016/j.ejca.2005.08.020

Cited by 49 publications

(64 citation statements)

References 107 publications

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“…These reports suggest that WWP1 may inhibit RNF11's function. Interestingly, RNF11 was also reported to inhibit EGF signaling by promoting EGFR endocytosis and degradation (Azmi and Seth, 2005;Burger et al, 2006). Indeed, we found that RNF11 siRNA increases both ErbB2 and EGFR and promotes cell proliferation in MCF10A ( Figure 5).…”

Section: Rnf11 Downregulates Erbb2 and Egfrmentioning

confidence: 69%

“…C Chen et al RNF11 is overexpressed in prostate and breast cancer cell lines Although RNF11 is a negative regulator of ErbB2 and EGFR, RNF11 has been reported to be overexpressed in breast cancer as detected by immunohistochemistry (IHC) Azmi and Seth, 2005). To confirm this result, we examined the RNF11 levels in breast cancer cell lines by qRT-PCR in 17 breast cancer …”

Section: Wwp1 Upregulates Erbb2 and Egfr Through Rnf11mentioning

confidence: 91%

“…RNF11 has a PY motif and has been shown to be an interacting protein of the HECTtype E3s Smurf2 and Itch Subramaniam et al, 2003). By yeast two-hybrid, RNF11 was also shown to interact with WWP1 (Azmi and Seth, 2005). However, complete analysis of the relationship between WWP1 and RNF11 has been lacking, although both proteins were implicated in breast and prostate cancers.…”

Section: Introductionmentioning

confidence: 99%

“…RNF11 was proposed to enhance EGFR degradation (Azmi and Seth, 2005;Burger et al, 2006). RNF11 has a PY motif and has been shown to be an interacting protein of the HECTtype E3s Smurf2 and Itch Subramaniam et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

“…Really interesting new gene (RING) finger protein 11 (RNF11) is a small RING finger-type E3 ligase whose expression was deregulated in breast tumors Azmi and Seth, 2005). RNF11 was proposed to enhance EGFR degradation (Azmi and Seth, 2005;Burger et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

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The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11

et al. 2008

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The WW domain containing E3 ubiquitin protein ligase 1 (WWP1) is a homologous to the E6-associated protein C terminus-type E3 ligase frequently overexpressed in human prostate and breast cancers due to gene amplification. Previous studies suggest that WWP1 promotes cell proliferation and survival; however, the mechanism of WWP1 action is still poorly understood. Here, we showed that WWP1 upregulates and maintains erythroblastic leukemia viral oncogene homolog 2 (ErbB2) and epithelial growth factor receptor (EGFR) in multiple cell lines. WWP1 depletion dramatically attenuates the EGFinduced ERK phosphorylation. WWP1 forms a protein complex with RING finger protein 11 (RNF11), a negative regulator of ErbB2 and EGFR. The proteinprotein interaction is through the first and third WW domains of WWP1 and the PY motif of RNF11. Although WWP1 is able to ubiquitinate RNF11 in vitro and in vivo, WWP1 neither targets RNF11 for degradation nor changes RNF11's cellular localization. Importantly, inhibition of RNF11 can rescue WWP1 siRNA-induced ErbB2 and EGFR downregulation and growth arrest. Finally, we demonstrated that RNF11 is overexpressed in a panel of prostate and breast cancer cell lines with WWP1 expression. These findings suggest that WWP1 may promote cell proliferation and survival partially through suppressing RNF11-mediated ErbB2 and EGFR downregulation.

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Section: Rnf11 Downregulates Erbb2 and Egfrmentioning

confidence: 69%

Section: Wwp1 Upregulates Erbb2 and Egfr Through Rnf11mentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11

et al. 2008

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

et al. 2018

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The Really Interesting New Gene (RING) Finger protein 11 (RNF11) is a subunit of the A20 ubiquitin-editing complex that ensures the transient nature of inflammatory responses. Although the role of RNF11 as a negative regulator of NF-κB signalling is well-documented, the molecular mechanisms that underpin this function are poorly understood. Here, we show that RNF11 binds both Ubc13 and the Ubc13~ubiquitin conjugate tightly and with similar affinity, but has minimal E3 ligase activity. Remarkably, RNF11 appears to bind Ubc13 so tightly that it outcompetes the E1 and an active E3 ligase. As a consequence, RNF11 may regulate the activity of E3s that rely on Ubc13 for ubiquitin chain assembly by limiting the availability of Ubc13 and its conjugate.

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Expression profiling of CD133⁺ and CD133^— epithelial cells from human prostate

et al. 2008

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RNF11 is a multifunctional modulator of growth factor receptor signalling and transcriptional regulation

Cited by 49 publications

References 107 publications

The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11

The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11

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

Expression profiling of CD133⁺ and CD133^— epithelial cells from human prostate

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RNF11 is a multifunctional modulator of growth factor receptor signalling and transcriptional regulation

Cited by 49 publications

References 107 publications

The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11

The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11

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

Expression profiling of CD133+ and CD133— epithelial cells from human prostate

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Expression profiling of CD133⁺ and CD133^— epithelial cells from human prostate