P2RX6

Official Full Name

purinergic receptor P2X 6

Organism

Homo sapiens

GeneID

9127

Background

The protein encoded by this gene belongs to the family of P2X receptors, which are ATP-gated ion channels and mediate rapid and selective permeability to cations. This gene is predominantly expressed in skeletal muscle, and regulated by p53. The encoded protein is associated with VE-cadherin at the adherens junctions of human umbilical vein endothelial cells. Alternative splicing results in multiple transcript variants. A related pseudogene, which is also located on chromosome 22, has been identified. [provided by RefSeq, Apr 2009]

Synonyms

P2X6; P2XM; P2RXL1;

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Detailed Information

As the most lethal one of all urological malignancies, renal cell carcinoma (RCC), is estimated to be with 65340 new cases and 14970 deaths for 2018 in the United States alone, and accounting for about 3.8% of all new malignancies. However, radiotherapy and chemotherapy accompanied with resection are currently basic solution for RCC. Although antiangiogenic therapy is the standard treatment for metastatic RCC (mRCC) and has improved patients' prognosis, but drug resistance hindered its effect. So, it is urgent to figure out more clinical indicator or therapeutic target for RCC metastasis through elucidation of the underlying mechanisms of earlier metastasis of RCC.

ATP is the main form of intracellular energy for all types of cells and and work as important roles in multiple cancer development. In physiological and pathological conditions, it can be released out into extracellular, where it can activate P2 receptors to mediate multiple biological functions. Two subfamilies' members of P2 receptors, P2X and P2Y, can be found in mammalian cells, and P2X family of ligand-gated ion channel receptors composited by seven members, P2RX1-7. And P2Y family of G protein-coupled receptors included by P2RY1,2,4,6,11,12,13,14, which has involvement in the two pathways, adenylate cyclase-cyclic adenosine 3',5'-monphosphate pathway and phospholipase C(PLC)-Ca²⁺ signaling pathway. Previous studies have reported the involvement of purinergic receptor subtypes in prostate, bladder, breast tumors, and P2RX6, a preferred receptor for ATP, was found to be making contributions to the invasion and metastasis of RCC cells.

Previous studies have shown cell migration and invasion of many human cancers can be promoted by extracellular ATP. But there are still poor understandings about the pro-invasive mechanisms of ATP and P2RX6, a preferred receptor for ATP. So biological function of P2RX6 in RCC progression was explored in the bioinformatics analysis such as IHC staining, tissue microarray and identification of differentially expressed genes in different stages of RCC. And it was found that RCC cells migration and invasion can be increased by ATP, and mechanism of this phenomenon can be dissected as Ca²⁺ mediated p-ERK1/2/MMP9 signali9ng regulated by ATP-P2RX6 to increase the RCC cells migration and invasion, and METTL14 implicated m6A modification in RCC and down-regulated P2RX6. Designing small molecules for targeting the newly identified ATP-P2RX6-Ca²⁺-p-ERK1/2-MMP9 signaling may be meaningful in the development of better approach to suppress RCC progression.

P2RX6 Figure 1. The illustration of ATP-P2RX6-Ca²⁺-p-ERK1/2-MMP9 signaling in the migration and invasion of RCC (renal cancer cell) (Gong et al., 2019).

References:

Dongkui Gong, Jin Zhang, Yonghui Chen, et al. The m6A-suppressed P2RX6 activation promotes renal cancer cells migration and invasion through ATP-induced Ca2+ influx modulating ERK1/2 phosphorylation and MMP9 signaling pathway. Journal of Experimental & Clinical Cancer Research, doi: 10.1186/s13046-019-1223-y.
Shui-Ping Liu, Qiujie Li, Ke Chen, et al. The emerging molecular mechanism of m6A modulators in tumorigenesis and cancer progression. Biomedicine & pharmacotherapie, doi: 10.1016/j.biopha.2020.110098.
Greig AV, Linge C, Healy V, et al. Expression of purinergic receptors in non-melanoma skin cancers and their functional roles in A431 cells. J Invest Dermatol. 2003;121: 315-27.

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