TRIM65 supports bladder urothelial carcinoma cell aggressiveness by promoting ANXA2 ubiquitination and degradation

Wen, Wei; Chen, Xin; Guo, Li; Li, Xiangzhong; Ming, Deng; Yuan, Gang; He, Lan; Li, Yong Hong; Zhang, Zhi Lin; Jiang, Li; Chen, Ri Xin; Xiao, Dan; Shi, Wei; Fang, Ning; Liu, Zhuo Wei; Luo, Jun; Zhou, Fangjian; Xie, Dan

doi:10.1016/j.canlet.2018.07.036

Cited by 56 publications

(43 citation statements)

References 30 publications

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“…Then, Western blots showed that the protein level of ANXA2 was decreased when S100A11 inhibition, while ANXA2 was increased when S100A11 overexpression (Figure A). Previously, studies reported that reported ANXA2 degradation was regulated by poly/multi‐ubiquitin . We wondered whether knockdown of S100A11‐induced ANXA2 decreased through the ubiquitin–proteasome pathway.…”

Section: Resultsmentioning

confidence: 97%

“…Previously, studies reported that reported ANXA2 degradation was regulated by poly/ multi-ubiquitin. 23 We wondered whether knockdown of S100A11induced ANXA2 decreased through the ubiquitin-proteasome pathway. To detect the role of the proteasome in ANXA2 degradation, U87 cells were transfected with sh-S100A11-1, sh-S100A11-2 or shCtrl and treated with the proteasome inhibitor, MG132.…”

Section: S100a11 Stabilizes Anxa2 In Gbm Cells By Decreasing Ubiquimentioning

confidence: 99%

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S100A11 functions as novel oncogene in glioblastoma via S100A11/ANXA2/NF‐κB positive feedback loop

Xie

et al. 2019

J Cellular Molecular Medi

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Glioblastoma (GBM) is the most universal type of primary brain malignant tumour, and the prognosis of patients with GBM is poor. S100A11 plays an essential role in tumour. However, the role and molecular mechanism of S100A11 in GBM are not clear. Here, we found that S100A11 was up‐regulated in GBM tissues and higher S100A11 expression indicated poor prognosis of GBM patients. Overexpression of S100A11 promoted GBM cell growth, epithelial‐mesenchymal transition (EMT), migration, invasion and generation of glioma stem cells (GSCs), whereas its knockdown inhibited these activities. More importantly, S100A11 interacted with ANXA2 and regulated NF‐κB signalling pathway through decreasing ubiquitination and degradation of ANXA2. Additionally, NF‐κB regulated S100A11 at transcriptional level as a positive feedback. We also demonstrated the S100A11 on tumour growth in GBM using an orthotopic tumour xenografting. These data demonstrate that S100A11/ANXA2/NF‐κB positive feedback loop in GBM cells that promote the progression of GBM.

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Section: Resultsmentioning

confidence: 97%

Section: S100a11 Stabilizes Anxa2 In Gbm Cells By Decreasing Ubiquimentioning

confidence: 99%

S100A11 functions as novel oncogene in glioblastoma via S100A11/ANXA2/NF‐κB positive feedback loop

Xie

et al. 2019

J Cellular Molecular Medi

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“…Several reports have indicated that TRIM65 is an oncogene in several cancers. For instance, Wei et al reported that TRIM65 increases progression of bladder urothelial carcinoma through upregulating ANXA2 degradation (Wei et al, ). J. Wang et al () indicated that TRIM65 is an oncogene in human lymphoma malignancies.…”

Section: Discussionmentioning

confidence: 99%

LncRNA LINC01857 promotes growth, migration, and invasion of glioma by modulating miR‐1281/TRIM65 axis

Liu

Wang³

et al. 2019

Journal Cellular Physiology

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The great importance of long noncoding RNAs (lncRNAs) has been acknowledged in tumorigenesis gradually. LncRNA LINC01857 is a novel lncRNA and has been reported to promote breast cancer progression. However, the biological roles of LINC01857 in glioma are not explored. In the present research, LINC01857 levels were found to be upregulated in glioma. In addition, LINC01857 expression is negatively correlated with survival rate in glioma patients. Functional investigation revealed that LINC01857 downregulation impaired glioma proliferation and invasiveness. Furthermore, LINC01857 knockdown led to repressed growth of glioma in vivo. We found that LINC01857 could be a sponge for miR-1281 and inhibits its level to upregulate TRIM65 expression. Whatʼs more, we showed that miR-1281 mimics also attenuated tumor cell proliferation, migration, and invasion.And rescue assays demonstrated that LINC01857 promotes glioma progression through modulating miR-1281/TRIM65 pathway. Collectively, this study first demonstrated that a novel LINC01857/miR-1281/TRIM65 signaling regulates glioma progression.

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“…Despite the broadly described role of Annexin A2 as a poor-prognosis marker during cancer progression, it has recently been reported to be induced for degradation by other oncogenic E3 ubiquitin-ligases, such as TRIM65 [38,39]. Furthermore, Annexin A2, involved in the membrane-cytoskeleton dynamics, was demonstrated to play a role in the recovery of E-cadherin at adherens junctions due to its effect on actin cytoskeleton [40], further supporting the above-explained phenotype observed during geldanamycin treatment.…”

Section: Discussionmentioning

confidence: 99%

Heat Shock Protein 90 Chaperone Regulates the E3 Ubiquitin-Ligase Hakai Protein Stability

Díaz-Díaz

Roca-Lema

Casas-Pais

et al. 2020

Cancers

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The E3 ubiquitin-ligase Hakai binds to several tyrosine-phosphorylated Src substrates, including the hallmark of the epithelial-to-mesenchymal transition E-cadherin, and signals for degradation of its specific targets. Hakai is highly expressed in several human cancers, including colon cancer, and is considered as a drug target for cancer therapy. Here, we report a link between Hakai and the heat shock protein 90 (Hsp90) chaperone complex. Hsp90 participates in the correct folding of its client proteins, allowing them to maintain their stability and activity. Hsp90 inhibitors specifically interfere with the association with its Hsp90 client proteins, and exhibit potent anti-cancer properties. By immunoprecipitation, we present evidence that Hakai interacts with Hsp90 chaperone complex in several epithelial cells and demonstrate that is a novel Hsp90 client protein. Interestingly, by overexpressing and knocking-down experiments with Hakai, we identified Annexin A2 as a Hakai-regulated protein. Pharmacological inhibition of Hsp90 with geldanamycin results in the degradation of Hakai in a lysosome-dependent manner. Interestingly, geldanamycin-induced Hakai degradation is accompanied by an increased expression of E-cadherin and Annexin A2. We also show that geldanamycin suppresses cell motility at least in part through its action on Hakai expression. Taken together, our results identify Hakai as a novel Hsp90 client protein and shed light on the regulation of Hakai stability. Our results open the possibility to the potential use of Hsp90 inhibitors for colorectal cancer therapy through its action on Hakai client protein of Hsp90.

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TRIM65 supports bladder urothelial carcinoma cell aggressiveness by promoting ANXA2 ubiquitination and degradation

Cited by 56 publications

References 30 publications

S100A11 functions as novel oncogene in glioblastoma via S100A11/ANXA2/NF‐κB positive feedback loop

S100A11 functions as novel oncogene in glioblastoma via S100A11/ANXA2/NF‐κB positive feedback loop

LncRNA LINC01857 promotes growth, migration, and invasion of glioma by modulating miR‐1281/TRIM65 axis

Heat Shock Protein 90 Chaperone Regulates the E3 Ubiquitin-Ligase Hakai Protein Stability

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