Pseudophosphatase STYX promotes tumor growth and metastasis by inhibiting FBXW7 function in colorectal cancer

He, Diao; Ma, Zongqing; Fang, Chao; Ding, Jingjing; Yang, Wenming; Chen, Peng; Huang, Libin; Wang, Cun; Yu, Yanyan; Yang, Lie; Li, Yuan; Zhou, Zong‐Guang

doi:10.1016/j.canlet.2019.04.014

Cited by 19 publications

(24 citation statements)

References 44 publications

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“…Precious studies have found that STYX can act as an oncogene in colorectal cancer [30]. Here, STYX was Fig.…”

Section: Discussionmentioning

confidence: 83%

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LncRNA SNHG6 enhances the radioresistance and promotes the growth of cervical cancer cells by sponging miR-485-3p

Liu

Liu²,

2020

Cancer Cell Int

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Background: Cervical cancer (CC) is the one of most common malignant gynecological tumors, which is characterized with the high mortality and recurrence rate. Previous studies have elucidated the oncogenic role of small nucleolar RNA host gene 6 (SNHG6) in some types of human cancers, whereas it is unclear whether it functions as an oncogene in CC. This study was aimed at unveiling the role of SNHG6 in CC. Methods: qRT-PCR analysis was implemented to evaluate the expression levels of SNHG6, miR-485-3p and STYX in CC cells. RNA pull down assay and luciferase reporter assay were conducted to verify the interaction between miR-485-3p and SNHG6 or STYX. Functional assays, such as colony formation assay, JC-1 assay and TUNEL assay were applied to detect the biological behaviors of CC cells. The resistance of CC cells to radiation was evaluated by colony formation assay. Results: SNHG6 was expressed at a high level in CC cells. Silenced SNHG6 suppressed cell proliferation but promoted cell apoptosis. Additionally, silenced SNHG6 could sensitize CC cells to radiation treatment. miR-485-3p could bind to both SNHG6 and STYX. Knockdown of miR-485-3p or overexpression of STYX could abolish the effects of SNHG6 silencing on CC cell growth. Conclusions: LncRNA SNHG6 enhances the radioresistance of CC cells and promotes CC cell growth by sponging miR-485-3p to release STYX.

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“…Precious studies have found that STYX can act as an oncogene in colorectal cancer [30]. Here, STYX was Fig.…”

Section: Discussionmentioning

confidence: 83%

“…Precious studies have found that STYX can act as an oncogene in colorectal cancer [ 30 ]. Here, STYX was explored as the downstream target of miR-485-3p in CC.…”

Section: Discussionmentioning

confidence: 99%

LncRNA SNHG6 enhances the radioresistance and promotes the growth of cervical cancer cells by sponging miR-485-3p

Liu

Liu²,

2020

Cancer Cell Int

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“…Furthermore, we found that breast cancer patient survival inversely correlated with low FBXW7 and high STYX levels. The relevance of the STYX‐FBXW7 crosstalk in cancer has been recently validated by an independent group for colon cancer [27]. Besides the biomedical implications of this finding, it demonstrated for the first time that the assembly of an SCF complex is regulated by a direct protein–protein interaction.…”

Section: Pseudoenzymes Within the Cc1‐fold Phosphatase Familymentioning

confidence: 88%

The dead phosphatases society: a review of the emerging roles of pseudophosphatases

et al. 2020

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Phosphatases are a diverse family of enzymes, comprising at least 10 distinct protein folds. Like most other enzyme families, many have sequence variations that predict an impairment or loss of catalytic activity classifying them as pseudophosphatases. Research on pseudoenzymes is an emerging area of interest, with new biological functions repurposed from catalytically active relatives. Here, we provide an overview of the pseudophosphatases identified to date in all major phosphatase families. We will highlight the degeneration of the various catalytic sequence motifs and discuss the challenges associated with the experimental determination of catalytic inactivity. We will also summarize the role of pseudophosphatases in various diseases and discuss the major challenges and future directions in this field.

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“…Drug development to stabilize the DPN–triloop interaction is a possible strategy to benefit cancer treatment. However, some of the members participate in the promotion of cancer development, such as STYX, SSH1, and SSH3 [ 34 , 35 , 36 ]. Drug development requires more structural information for support, and our studies may serve as a foundation for further investigation of treatments focusing on N-loop-containing PTPs.…”

Section: Discussionmentioning

confidence: 99%

Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases

Lai

Chang

Chuang

et al. 2020

IJMS

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Cysteine-based protein tyrosine phosphatases (Cys-based PTPs) perform dephosphorylation to regulate signaling pathways in cellular responses. The hydrogen bonding network in their active site plays an important conformational role and supports the phosphatase activity. Nearly half of dual-specificity phosphatases (DUSPs) use three conserved residues, including aspartate in the D-loop, serine in the P-loop, and asparagine in the N-loop, to form the hydrogen bonding network, the D-, P-, N-triloop interaction (DPN–triloop interaction). In this study, DUSP22 is used to investigate the importance of the DPN–triloop interaction in active site formation. Alanine mutations and somatic mutations of the conserved residues, D57, S93, and N128 substantially decrease catalytic efficiency (kcat/KM) by more than 102-fold. Structural studies by NMR and crystallography reveal that each residue can perturb the three loops and induce conformational changes, indicating that the hydrogen bonding network aligns the residues in the correct positions for substrate interaction and catalysis. Studying the DPN–triloop interaction reveals the mechanism maintaining phosphatase activity in N-loop-containing PTPs and provides a foundation for further investigation of active site formation in different members of this protein class.

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Pseudophosphatase STYX promotes tumor growth and metastasis by inhibiting FBXW7 function in colorectal cancer

Cited by 19 publications

References 44 publications

LncRNA SNHG6 enhances the radioresistance and promotes the growth of cervical cancer cells by sponging miR-485-3p

LncRNA SNHG6 enhances the radioresistance and promotes the growth of cervical cancer cells by sponging miR-485-3p

The dead phosphatases society: a review of the emerging roles of pseudophosphatases

Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases

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