A SIX1 degradation inducer blocks excessive proliferation of prostate cancer

Liao, Yuning; Sun, Wenshuang; Shao, Zhenlong; Liu, Yuan; Zhong, Xiaoyu; Deng, Yuanfei; Liu, Fang; Huang, Hongbiao; Liu, Jinbao

doi:10.7150/ijbs.67873

Cited by 7 publications

(3 citation statements)

References 43 publications

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“…The SIX1 (sine oculis homeobox homolog 1) is a poor prognostic indicator in PCa. USP1 can interact with SIX1 and stabilize its protein levels in a GRP75 (glucose regulated protein 75)-dependent manner, thereby promoting the cellular proliferation and castration resistance of PCa ( Liao et al, 2021a ; Liao et al, 2022 ).…”

Section: Survey Methodologymentioning

confidence: 99%

Ubiquitin specific peptidases and prostate cancer

Guo

Cui

Chen

et al. 2023

PeerJ

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Protein ubiquitination is an important post-translational modification mechanism, which regulates protein stability and activity. The ubiquitination of proteins can be reversed by deubiquitinating enzymes (DUBs). Ubiquitin-specific proteases (USPs), the largest DUB subfamily, can regulate cellular functions by removing ubiquitin(s) from the target proteins. Prostate cancer (PCa) is the second leading type of cancer and the most common cause of cancer-related deaths in men worldwide. Numerous studies have demonstrated that the development of PCa is highly correlated with USPs. The expression of USPs is either high or low in PCa cells, thereby regulating the downstream signaling pathways and causing the development or suppression of PCa. This review summarized the functional roles of USPs in the development PCa and explored their potential applications as therapeutic targets for PCa.

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Section: Survey Methodologymentioning

confidence: 99%

Ubiquitin specific peptidases and prostate cancer

Guo

Cui

Chen

et al. 2023

PeerJ

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“…This assay was performed with at least three independent repeats, as described before. [25] Immunofluorescence Assay: Cells were seeded in a chamber slide and transfected with HA-STUB1 plasmids for 48 h. Next, they were washed, fixed, permeabilized, and blocked, as previously reported. [26] The primary antibodies anti-HA tag, anti-YTHDF2, and anti-HSP90𝛽 were used to bind the specific proteins.…”

Section: Methodsmentioning

confidence: 99%

HSP90β Impedes STUB1‐Induced Ubiquitination of YTHDF2 to Drive Sorafenib Resistance in Hepatocellular Carcinoma

Liao

Liu

et al. 2023

Advanced Science

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YTH domain family 2 (YTHDF2) is the first identified N6‐methyladenosine (m6A) reader that regulates the status of mRNA. It has been reported that overexpressed YTHDF2 promotes carcinogenesis; yet, its role in hepatocellular carcinoma (HCC) is elusive. Herein, it is demonstrated that YTHDF2 is upregulated and can predict poor outcomes in HCC. Decreased ubiquitination levels of YTHDF2 contribute to the upregulation of YTHDF2. Furthermore, heat shock protein 90 beta (HSP90β) and STIP1 homology and U‐box‐containing protein 1 (STUB1) physically interact with YTHDF2 in the cytoplasm. Mechanically, the large and small middle domain of HSP90β is required for its interaction with STUB1 and YTHDF2. HSP90β inhibits the STUB1‐induced degradation of YTHDF2 to elevate the expression of YTHDF2 and to further boost the proliferation and sorafenib resistance of HCC. Moreover, HSP90β and YTHDF2 are upregulated, while STUB1 is downregulated in HCC tissues. The expression of HSP90β is positively correlated with the YTHDF2 protein level, whereas the expression of STUB1 is negatively correlated with the protein levels of YTHDF2 and HSP90β. These findings deepen the understanding of how YTHDF2 is regulated to drive HCC progression and provide potential targets for treating HCC.

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“…However, increasing evidence has been suggesting that this effect is not at the transcriptional level but is directly related to the increased protein stability of SIX1 [244]. In concordance, it was shown that triggering SIX1 degradation using a chemical inducer results in inhibition of cell growth and sensitization of PCa cells to enzalutamidemediated castration [245]. In addition, increased SIX1 protein level causes a decrease in the E-cadherin and an increase in the N-cadherin levels [246,247].…”

Section: Forkhead Box Protein C2 (Foxc2)mentioning

confidence: 96%

Dissecting the effects of androgen deprivation therapy on cadherin switching in advanced prostate cancer: A molecular perspective

Varisli¹,

TOLAN²,

CEN³

et al. 2022

Oncology Research

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Prostate cancer is one of the most often diagnosed malignancies in males and its prevalence is rising in both developed and developing countries. Androgen deprivation therapy has been used as a standard treatment approach for advanced prostate cancer for more than 80 years. The primary aim of androgen deprivation therapy is to decrease circulatory androgen and block androgen signaling. Although a partly remediation is accomplished at the beginning of treatment, some cell populations become refractory to androgen deprivation therapy and continue to metastasize.Recent evidences suggest that androgen deprivation therapy may cause cadherin switching, from E-cadherin to Ncadherin, which is the hallmark of epithelial-mesenchymal transition. Diverse direct and indirect mechanisms are involved in this switching and consequently, the cadherin pool changes from E-cadherin to N-cadherin in the epithelial cells. Since E-cadherin represses invasive and migrative behaviors of the tumor cells, the loss of E-cadherin disrupts epithelial tissue structure leading to the release of tumor cells into surrounding tissues and circulation. In this study, we review the androgen deprivation therapy-dependent cadherin switching in advanced prostate cancer with emphasis on its molecular basis especially the transcriptional factors regulated through TFG-β pathway.

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A SIX1 degradation inducer blocks excessive proliferation of prostate cancer

Cited by 7 publications

References 43 publications

Ubiquitin specific peptidases and prostate cancer

Ubiquitin specific peptidases and prostate cancer

HSP90β Impedes STUB1‐Induced Ubiquitination of YTHDF2 to Drive Sorafenib Resistance in Hepatocellular Carcinoma

Dissecting the effects of androgen deprivation therapy on cadherin switching in advanced prostate cancer: A molecular perspective

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