ECD promotes gastric cancer metastasis by blocking E3 ligase ZFP91-mediated hnRNP F ubiquitination and degradation

Xu, Songhui; Zhu, Shuguang; Wang, Yanjie; Huang, Jinzhou; Chen, Min; Wu, Qingxia; He, Yutian; Chen, De; Yan, Guang-Rong

doi:10.1038/s41419-018-0525-x

Cited by 29 publications

(38 citation statements)

References 31 publications

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“…This procedure was carried out as previously described. 21 Briefly, cells were cotransfected with the indicated plasmids for 24 hours, and were treated with 10 μmol/L MG132 for the indicated number of hours prior to harvesting. Cells were lysed in RIPA buffer containing protease inhibitor cocktail (Roche).…”

Section: In Vivo Ubiquitination Assaymentioning

confidence: 99%

“…Expression plasmids containing pCMV-Flag-STUB1, pCMV-Myc-STUB1, pCMV-Flag-YAP1, and pCMV-Myc-YAP1 were constructed as previously described, 20 and the different Flag-tagged STUB1 fragments and mutations were generated as previously described. 21 The HA-tagged ubiquitin (HA-ub) plasmid and mutation constructs were kindly provided by Professor Jianfei Qi from the University of Maryland Cancer Center. Mutations were produced using a QuikChange Site-Directed Mutagenesis Kit (Stratagene) and validated by DNA sequencing.…”

Section: Introductionmentioning

confidence: 99%

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RETRACTED: STUB1 suppresseses tumorigenesis and chemoresistance through antagonizing YAP1 signaling

et al. 2019

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Yes‐associated protein (YAP) is a component of the canonical Hippo signaling pathway that is known to play essential roles in modulating organ size, development, and tumorigenesis. Activation or upregulation of YAP1, which contributes to cancer cell survival and chemoresistance, has been verified in different types of human cancers. However, the molecular mechanism of YAP1 upregulation in cancer is still unclear. Here we report that the E3 ubiquitin ligase STUB1 ubiquitinates and destabilizes YAP1, thereby inhibiting cancer cell survival. Low levels of STUB1 expression were correlated with increased protein levels of YAP1 in human gastric cancer cell lines and patient samples. Moreover, we revealed that STUB1 ubiquitinates YAP1 at the K280 site by K48‐linked polyubiquitination, which in turn increases YAP1 turnover and promotes cellular chemosensitivity. Overall, our study establishes YAP1 ubiquitination and degradation mediated by the E3 ligase STUB1 as an important regulatory mechanism in gastric cancer, and provides a rationale for potential therapeutic interventions.

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Section: In Vivo Ubiquitination Assaymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

RETRACTED: STUB1 suppresseses tumorigenesis and chemoresistance through antagonizing YAP1 signaling

et al. 2019

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“…The eluted samples were subject to in‐solution trypsin digestion, liquid chromatography‐mass spectrometry (MS) analysis and database search by the proteomic service of Shenzhen University. Identities of the coprecipitated proteins were determined as described previously 20 …”

Section: Methodsmentioning

confidence: 99%

RETRACTED: Targeting USP1‐dependent KDM4A protein stability as a potential prostate cancer therapy

et al. 2020

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Abbreviations: AR, androgen receptor; ARE, androgen-responsive element; DUB, deubiquitinating enzyme; H3K9, histone H3 on lysine 9; H3K36, histone H3 on lysine 36; HA-ub, HA-tagged ubiquitin; IB, immunoblot; IHC, immunohistochemistry; IP, immunoprecipitation; KDM4A, lysine-specific demethylase 4A; PC, prostate cancer; PTEN, phosphatase and tensin homolog; qPCR, quantitative PCR. AbstractThe histone demethylase lysine-specific demethylase 4A (KDM4A) is reported to be overexpressed and plays a vital in multiple cancers through controlling gene expression by epigenetic regulation of H3K9 or H3K36 methylation marks. However, the biological role and mechanism of KDM4A in prostate cancer (PC) remain unclear.Herein, we reported KDM4A expression was upregulation in phosphatase and tensin homolog knockout mouse prostate tissue. Depletion of KDM4A in PC cells inhibited their proliferation and survival in vivo and vitro. Further studies reveal that USP1 is a deubiquitinase that regulates KDM4A K48-linked deubiquitin and stability.Interestingly, we found c-Myc was a key downstream effector of the USP1-KDM4A/ androgen receptor axis in driving PC cell proliferation. Notably, upregulation of KDM4A expression with high USP1 expression was observed in most prostate tumors and inhibition of USP1 promotes PC cells response to therapeutic agent enzalutamide. Our studies propose USP1 could be an anticancer therapeutic target in PC.

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“…ZFP91 has been reported to play an important role in cancer progression and tumorigenesis, especially in GC. 39,40 Peng et al showed that ZEP91 was a target of miR-188-5p and together with it regulated GC cell proliferation and invasion. 41 In our study, ZFP91 was a target mRNA of miR-22-3p and overexpression of ZFP91 could alleviate the inhibitory effect of overexpression of miR-22-3p on GC/OXA cells.…”

Section: Discussionmentioning

confidence: 99%

<p>lncRNA MALAT1 modulates oxaliplatin resistance of gastric cancer via sponging miR-22-3p</p>

Zhang

2020

OTT

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Objective: Various regulatory mechanisms have been demonstrated to be associated with cancer progression. ncRNA and mRNA play important roles in gastric cancer (GC) cell growth and drug resistance, respectively. However, the regulatory network of ncRNA and mRNA in GC oxaliplatin (OXA) resistance has not been fully clarified. Methods: The expression of miR-22-3p, MALAT1, and zinc finger protein 91 (ZFP91) was detected in tissues and cells using quantitative real-time PCR. The protein level of ZFP91 was measured by Western blot analysis. Luciferase reporter, pull-down, and RNA immunoprecipitation assays were used to determine the relationship between MALAT1, miR-22-3p, and ZFP91. MTT assay was applied to measure cell survival and proliferation. Cell apoptosis was detected using flow cytometry. Tumor xenograft assay was used to detect the function of miR-22-3p in vivo. Results: In this study, we found that MALAT1 and ZFP91 expression was upregulated while the expression of miR-22-3p was downregulated in GC/OXA tissues and cells. Additionally, miR-22-3p was a target miRNA of MALAT1 and ZFP91 was a target mRNA of miR-22-3p. Functional studies showed that the knockdown of MALAT1 or overexpression of miR-22-3p inhibited GC/OXA cell survival, proliferation, and drug resistance as well as induced apoptosis, which could be reversed by the inhibition of miR-22-3p or overexpression of ZFP91. Conclusion: We observed a new regulatory network for MALAT1 in drug resistance of GC. MALAT1 modulates ZFP91 to promote GC cells OXA resistance via sponging miR-22-3p.

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ECD promotes gastric cancer metastasis by blocking E3 ligase ZFP91-mediated hnRNP F ubiquitination and degradation

Cited by 29 publications

References 31 publications

RETRACTED: STUB1 suppresseses tumorigenesis and chemoresistance through antagonizing YAP1 signaling

RETRACTED: STUB1 suppresseses tumorigenesis and chemoresistance through antagonizing YAP1 signaling

RETRACTED: Targeting USP1‐dependent KDM4A protein stability as a potential prostate cancer therapy

<p>lncRNA MALAT1 modulates oxaliplatin resistance of gastric cancer via sponging miR-22-3p</p>

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