A novel HECT-type E3 ubiquitin protein ligase NEDL1 enhances the p53-mediated apoptotic cell death in its catalytic activity-independent manner

Li, Y; Ozaki, Toshinori; Kikuchi, Hiromi; Yamamoto, Hideki; Ohira, Miki; Nakagawara, Akira

doi:10.1038/sj.onc.1211032

Cited by 53 publications

(55 citation statements)

References 27 publications

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“…RNF43 and NEDL1 likely have ubiquitin ligase activities because RNF43 and NEDL1 have a RING domain and a HECT domain, respectively. Overexpression of NEDL1 enhances p53-mediated transcription, suggesting that NEDL1 does not degrade p53 via the ubiquitin-proteasomal pathway [16]. On the other hand, we showed that RNF43 interacts with NEDL1 and inhibits p53-mediated transcription, suggesting that RNF43 is an E3 ubiquitin ligase for NEDL1 or p53.…”

Section: Discussionmentioning

confidence: 66%

“…Furthermore, it has been reported that NEDL1 interacts with p53 and enhances transcriptional activity of p53 and p53-mediated apoptotic cell death. These findings suggest that NEDL1 regulates cell proliferation and differentiation, stress responses, and DNA-damage responses [15,16].…”

Section: Introductionmentioning

confidence: 82%

“…It has been reported that NEDL1 interacts with p53 and enhances p53-mediated apoptotic cell death [16]. We examined whether RNF43 also interacts with p53.…”

Section: Interaction Of Rnf43 With P53mentioning

confidence: 97%

“…Since it has been reported that NEDL1 enhances transcriptional activity of p53 [16], we examined the effect of RNF43 on p53-mediated transcriptional activity. A luciferase reporter construct containing p53-responsive element were transfected with several amounts of RNF43 and/or p53 expression vectors into H1299 cells and the luciferase activity was measured.…”

Section: Rnf43 Suppresses P53 Mediated Transcriptional Activitymentioning

confidence: 99%

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RNF43 interacts with NEDL1 and regulates p53-mediated transcription

Shinada

Tsukiyama

Sho

et al. 2011

Biochemical and Biophysical Research Communications

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The ubiquitin-proteasomal system plays a crucial role in oncogenesis in colorectal tissues. Recent studies have shown that stability of -catenin, which functions as an oncogene for colorectal cancer, is regulated by ubiquitin-mediated degradation. It has been reported that a putative E3 ubiquitin ligase, RNF43, is highly expressed in human colorectal carcinoma and that RNF43 promotes cell growth. However, the involvement of RNF43 in carcinogenesis has not been fully elucidated. In this study, we found by using yeast two-hybrid screening that RNF43 binds to NEDD-4-like ubiquitin-protein ligase-1 (NEDL1), which enhances pro-apoptotic activity by p53. In addition, we found that RNF43 also interacts with p53 and that RNF43 suppresses transcriptional activity of p53 in H1299 cells and attenuates apoptosis induced by ultraviolet irradiation. These findings suggest that RNF43 is associated with p53-mediated apoptosis in collaboration with NEDL1 in colorectal carcinogenesis.3

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Section: Discussionmentioning

confidence: 66%

Section: Introductionmentioning

confidence: 82%

“…It has been reported that NEDL1 interacts with p53 and enhances p53-mediated apoptotic cell death [16]. We examined whether RNF43 also interacts with p53.…”

Section: Interaction Of Rnf43 With P53mentioning

confidence: 97%

Section: Rnf43 Suppresses P53 Mediated Transcriptional Activitymentioning

confidence: 99%

See 2 more Smart Citations

RNF43 interacts with NEDL1 and regulates p53-mediated transcription

Shinada

Tsukiyama

Sho

et al. 2011

Biochemical and Biophysical Research Communications

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“…Similar results were observed for HECW1. HECW1 (NEDL1) has been shown to be an E3 ligase for Dvl-1 (Miyazaki et al, 2004) and to cooperate with p53 to induce apoptosis independent of its E3 ligase activity (Li et al, 2008a). Thus, WWP1, Itch and HECW1 additively suppress the ErbB4 expression in some breast cancers.…”

Section: Discussionmentioning

confidence: 99%

WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer

Zhou

Alimandi

et al. 2009

Oncogene

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ErbB4, a member of the epidermal growth factor receptor family, plays a role in normal breast and breast cancer development by regulating mammary epithelial cell proliferation, survival and differentiation. In this study, we show that WWP1, a C2-WW-HECT type E3 ubiquitin ligase, binds, ubiquitinates and destructs ErbB4-CYT1, but much less efficiently for CYT2, isoforms (both JMa and JMb). The protein-protein interaction occurs primarily between the first and third WW domains of WWP1 and the second PY motif of ErbB4. Knockdown of WWP1 by two different small interfering RNAs increases the endogenous ErbB4 protein levels in both MCF7 and T47D breast cancer cell lines. In addition, overexpression of the wild type, but not the catalytic inactive WWP1, dramatically decreases the endogenous ErbB4 protein levels in MCF7. Importantly, we found that WWP1 negatively regulates the heregulin-b1-stimulated ErbB4 activity as measured by the serum response element report assay and the BRCA1 mRNA expression. After a systematic screening of all WWP1 family members by small interfering RNA, we found that AIP4/Itch and HECW1/NEDL1 also negatively regulate the ErbB4 protein expression in T47D. Interestingly, the protein expression levels of both WWP1 and ErbB4 are higher in estrogen receptor-a-positive than in estrogen receptor-anegative breast cancer cell lines. These data suggest that WWP1 and its family members suppress the ErbB4 expression and function in breast cancer.

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Genome‐wide high‐resolution analysis of DNA copy number alterations in NF1‐associated malignant peripheral nerve sheath tumors using 32K BAC array

Mantripragada

Ståhl

Patridge

et al. 2009

Genes Chromosomes & Cancer

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Neurofibromatosis Type I (NF1) is an autosomal dominant disorder characterized by the development of both benign and malignant tumors. The lifetime risk for developing a malignant peripheral nerve sheath tumor (MPNST) in NF1 patients is approximately 10% with poor survival rates. To date, the molecular basis of MPNST development remains unclear. Here, we report the first genome-wide and high-resolution analysis of DNA copy number alterations in MPNST using the 32K bacterial artificial chromosome microarray on a series of 24 MPNSTs and three neurofibroma samples. In the benign neurofibromas, apart from loss of one copy of the NF1 gene and copy number polymorphisms, no other changes were found. The profiles of malignant samples, however, revealed specific loss of chromosomal regions including 1p35-33, 1p21, 9p21.3, 10q25, 11q22-23, 17q11, and 20p12.2 as well as gain of 1q25, 3p26, 3q13, 5p12, 5q11.2-q14, 5q21-23, 5q31-33, 6p23-p21, 6p12, 6q15, 6q23-q24, 7p22, 7p14-p13, 7q21, 7q36, 8q22-q24, 14q22, and 17q21-q25. Copy number gains were more frequent than deletions in the MPNST samples (62% vs. 38%). The genes resident within common regions of gain were NEDL1 (7p14), AP3B1 (5q14.1), and CUL1 (7q36.1) and these were identified in >63% MPNSTs. The most frequently deleted locus encompassed CDKN2A, CDKN2B, and MTAP genes on 9p21.3 (33% cases). These genes have previously been implicated in other cancer conditions and therefore, should be considered for their therapeutic, prognostic, and diagnostic relevance in NF1 tumorigenesis.

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A novel HECT-type E3 ubiquitin protein ligase NEDL1 enhances the p53-mediated apoptotic cell death in its catalytic activity-independent manner

Cited by 53 publications

References 27 publications

RNF43 interacts with NEDL1 and regulates p53-mediated transcription

RNF43 interacts with NEDL1 and regulates p53-mediated transcription

WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer

Genome‐wide high‐resolution analysis of DNA copy number alterations in NF1‐associated malignant peripheral nerve sheath tumors using 32K BAC array

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