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EPB41L5 (erythrocyte membrane protein band 4.1 like 5) gene localization with human chromosome 2q14.2. This gene encodes the EPB41L5 protein, also known as BE37, YMO1. EPB41L5 is the first protein found in cytoskeleton and cell movement found in November 2007 and is widely expressed in the mesoderm and endoderm epithelial tissues of mammalian embryos. The dysregulation of EPB41L5 protein expression is closely related to the occurrence of some tumors.
Biological Function of EPB41L5
EPB41L5 belongs to the 4.1 protein family, which has a FERM domain at the N-terminus but lacks an actin-binding site at the C-terminus. The Band4.1 family is a very popular connexin family. Its large members of the family can participate in signal transduction. They also can connect with membrane proteins and cytosolic proteins (such as actin) of cells to exert stable cell structure.
EPB41L5 is involved in the development of the body and can play a role in TGF-β-induced EMT transformation by regulating the expression of downstream cadherin E-cadherin. The FERRM of EPB41L5 can interact with MPP5, CRB2, and CRB3 to form a CRB-MPP5-EPB41L5 complex. The complex can regulate a variety of cell adhesion factors, plays an important role in the tight junction between cells and the formation of cell polarity. Moreover, it is closely related to epithelial cell polarity and basement membrane formation. The FERM domain contained in EPB41L5 can cross-link with myosins protein containing MyThin tail homology 4 domain, and participate in cell pseudopod formation and cell movement. It also can bind to cytoskeletal proteins Talinl, PTK, and regulate cell actin skeleton.
When TGF-β stimulates cells, it up-regulates the expression of EPB41L5 and stimulates EMT. This process is mainly through up-regulation of EPB41L5, which competes with cell adhesion molecule E-cadherin for binding to p120-catenin, thereby reducing the cell surface adhesion molecule e-cadherin, which leads to cell separation. EPB41L5 enhances cell motility by enhancing adhesion spots at its C-terminus. In addition, EPB41L5 regulates the contractility of actomyosin by directly recruiting the small GTPase ARHGEF18, thereby affecting the focal adhesome (FA) maturation. This process is influenced by the composition of the extracellular matrix (ECM) and the potential regulation of collagen receptor mediated..
Figure 1. ECM influences EPB41L5-mediated phenotypes. (Schell C, et al. 2017)
EPB41L5 and Tumor
Studies have shown that EPB41L5 protein is highly expressed in the highly invasive renal clear cell carcinoma cell line 786-O and breast cancer cells MDA-MB-23. EPB41L5 protein forms Arf6-AMAP1-EPB41L5 complex with Arf6 and AMAP1 to Promote the invasion and metastasis of renal cancer cells to the stroma. The study found that EPB41L5 is also involved in the migration and invasion of tumor cells during cancer pathogenesis. Studies have reported a high correlation between EPB41L5 and lymph node metastasis in patients with head and neck squamous cell carcinoma and survival after surgery. Daimon et al. confirmed that the expression level of EPB41L5 was significantly increased in the translocation tissues of upper urinary tract cell carcinoma, and the highly expressed EPB41L5 was positively correlated with tumor grade, pathological stage, and tumor cell invasion.
The bioinformatics analysis and luciferase reporter gene assay confirmed that EPB41L5 was the target gene of miR-184, and the expression level of EPB41L5 was significantly decreased in renal cancer cells overexpressing miR-184. After EPB41L5 was silenced, the survival and migration ability of renal cancer cells was significantly decreased, indicating that the inhibitory effect of miR-184 on renal cell survival was achieved by regulating its target gene EPB41L5.