MYO6 knockdown inhibits the growth and induces the apoptosis of prostate cancer cells by decreasing the phosphorylation of ERK1/2 and PRAS40

Wang, Dong; Zhu, Lihong; Liao, Min; Zeng, Taidui; Zhuo, Wei; Yang, Shaodong; Wu, Wei

doi:10.3892/or.2016.4910

Cited by 31 publications

(27 citation statements)

References 27 publications

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“…[37][38][39] More than that, MYO6 has been verified to highly express in many cancers, such as prostate cancer, CRC, breast cancer and gastric cancer, which also participated in cell progression. [40][41][42][43] In our study, consistent with a previous study, miR-124 expressed low and MYO6 expressed high in CRC tissues and cells, and rescue experiments confirmed the effects of HNF1A-AS1 on cell migration and invasion through targeting miR-124/ MYO6 axis. More than that, glycolysis provides energy for the metabolism of tumor cells and guarantees the proliferation and development of tumor cells.…”

Section: Discussionsupporting

confidence: 92%

<p>HNF1A-AS1 Regulates Cell Migration, Invasion and Glycolysis via Modulating miR-124/MYO6 in Colorectal Cancer Cells</p>

Guo¹,

Zhang²,

Liu³

et al. 2020

OTT

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Background: Accumulating evidence determined that lncRNAs play multiple roles in cell progression in colorectal cancer (CRC). Long noncoding RNA (lncRNA) hepatocyte nuclear factor 1 homeobox A (HNF1A)-antisense RNA 1 (AS1) has been identified to affect cell growth and disease diagnosis in various cancers, including CRC. However, the underlying regulatory mechanism of HNF1A-AS1 in cell progression and glycolysis has not been fully explored in CRC. Materials and Methods: The expression of HNF1A-AS1, microRNA-124 (miR-124) and Myosins of class VI (MYO6) was detected using reverse transcription-quantitative polymerase chain reaction (RT-qPCR). The analysis of glucose consumption, lactate production and hexokinase 2 (HK2) protein level was used to assess glycolysis in cells. The protein level of HK2 and MYO6 was measured with Western blot. Cell migration and invasion were evaluated using the transwell assay. The relationship among HNF1A-AS1, miR-124 and MYO6 was determined via luciferase reporter and RNA immunoprecipitation (RIP) assay. Results: In this study, we found that HNF1A-AS1 was upregulated in CRC tissues and cell lines. Functional experiments determined that reduction of HNF1A-AS1 or promotion of miR-124 inhibited cell migration and invasion as well as glycolysis in CRC cells. What' more, luciferase reporter assay manifested that miR-124 was a target of HNF1A-AS1 and MYO6 was a target mRNA of miR-124 in CRC cells. Additionally, reverse experiments showed that the effects of si-HNF1A-AS1 on colorectal cancer cells were impaired by anti-miR-124 and the effects of high miR-124 expression on CRC cells were rescued by upregulating MYO6. HNF1A-AS1 regulated MYO6 expression via targeting miR-124 in CRC cells. Conclusion: In this study, we first found that HNF1A-AS1 regulated cell migration, invasion and glycolysis via modulating miR-124/MYO6 in CRC cells.

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Section: Discussionsupporting

confidence: 92%

<p>HNF1A-AS1 Regulates Cell Migration, Invasion and Glycolysis via Modulating miR-124/MYO6 in Colorectal Cancer Cells</p>

Guo¹,

Zhang²,

Liu³

et al. 2020

OTT

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“…We therefore propose that the function of myosin VI is particularly critical when cells are under high transcription load and undergo rapid changes in the gene expression landscape. This is consistent with previous observations of myosin VI being over-expressed in several cancers, along with interacting with nuclear receptors and participating in the expression of target genes (Dunn et al, 2006, Loikkanen et al, 2009, Puri et al, 2010, Wang et al, 2016, Wang et al, 2015, Wollscheid et al, 2016. With regard to the factories, various key questions remain unanswered, for instance how the clustering sites are selected and how they are brought together?…”

Section: Discussionsupporting

confidence: 90%

Nuclear myosin VI regulates the spatial organization of mammalian transcription initiation

Hari-Gupta

Fili

Santos

et al. 2020

Preprint

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During transcription, RNA Polymerase II (RNAPII) is spatially organised within the nucleus into clusters that correlate with transcription activity. While this is a hallmark of genome regulation in mammalian cells, the mechanisms concerning the assembly, organisation and stability which underpin the function these transcription factories remain unknown. Here, we have used combination of single molecule imaging and genomic approaches to explore the role of nuclear myosin VI in the nanoscale organisation of RNAPII. We reveal that myosin VI acts as the molecular anchor that holds RNAPII into transcription factories. Perturbation of myosin VI leads to the disruption of RNAPII localisation, changes in chromatin organisation and subsequently a decrease in gene expression. Overall, we uncover the fundamental role of myosin VI in the spatial regulation of gene expression during the rapid response to changes in the cellular environment.

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“…The dephosphorylation of PRAS40 and mTOR pathway by AMPK was found to be responsible for the apoptosis led by ATP-P2×7 signaling [ 61 ]. The phosphorylation of PRAS40 is downregulated by MYO6 knockdown which inhibits the growth and induces the apoptosis of prostate cancer cells [ 62 ]. Taken together, the anti-apoptotic role of PRAS40 is dependent on the suppression of mTOR signaling.…”

Section: Pras40 In Tumormentioning

confidence: 99%

PRAS40 signaling in tumor

Guo

Zhang

et al. 2017

Oncotarget

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The proline-rich Akt substrate of 40 kDa (PRAS40) is a substrate of Akt and a component of the mammalian target of rapamycin complex 1 (mTORC1). Locating at the crossroad of the PI3K/Akt pathway and the mTOR pathway, PRAS40 is phosphorylated by growth factors or other stimuli, and regulates the activation of these signaling pathways in turn. PRAS40 plays an important role in metabolic disorders and multiple cancers, and the phosphorylation of PRAS40 is often associated with the tumor progression of melanoma, prostate cancer, etc. PRAS40 promotes tumorigenesis by deregulating cellular proliferation, apoptosis, senescence, metastasis, etc. Herein, we provide an overview on current understandings of PRAS40 signaling in the tumor formation and progression, which suggests that PRAS40 or phospho-PRAS40 could become a novel biomarker and therapeutic target in tumor.

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MYO6 knockdown inhibits the growth and induces the apoptosis of prostate cancer cells by decreasing the phosphorylation of ERK1/2 and PRAS40

Cited by 31 publications

References 27 publications

<p>HNF1A-AS1 Regulates Cell Migration, Invasion and Glycolysis via Modulating miR-124/MYO6 in Colorectal Cancer Cells</p>

<p>HNF1A-AS1 Regulates Cell Migration, Invasion and Glycolysis via Modulating miR-124/MYO6 in Colorectal Cancer Cells</p>

Nuclear myosin VI regulates the spatial organization of mammalian transcription initiation

PRAS40 signaling in tumor

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