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EMP3 consists of two extracellular domains of 41 amino acids each, as well as three intracellular domains. It is highly conserved among the PMP22 protein family. The hydrophobic regions on the extracellular domain are remarkably similar to those on the PMP22 proteins. The ECD is a 13-amino acid loop, which contains a series of post-translational modifications. It also has two N-glycosylated residues at asparagine 47 and 56.
The phenotype of EMP3 expression can be determined by investigating its relationship to ErbB2/HER2 signaling. Activation of the EMP3 pathway by ErbB2 protein is associated with an increased level of this protein. Similarly, overexpression of EMP3 inhibits the activity of HER2-mediated transcription, and PI3K inhibitors have a similar effect on the ERBB2-HER2 pathway.
The EMP3 protein has been linked to the regulation of other ECM receptors. Overexpression of EMP3 in bladder cancer cells increased the levels of integrins and downstream FAK targets. This is consistent with the increased migration of bladder cancer cells, which may indicate that EMP3 has an important role in the progression of bladder cancer. The authors concluded that EMP3 overexpression may play a role in regulating the migration of these tumors.
The two major categories of EMP3 include extracellular domains and intracellular domains. The ECDs are composed of a 13 amino acid loop and a C-terminal tail that is short. The EMP3 protein has highly conserved hydrophobic regions in the PMP22 family of proteins. Further, it has a highly conserved structure among other members of the PMP22 protein family. The N- and C-terminal tails of EMP3s are highly conserved and are cytoplasmic.
The EMP3 gene is part of a 60-gene signature that is differentially expressed in cancer patients. In a study conducted at MSKCC, the EMP3 protein was found to be mainly present in the cytoplasm. However, the exact location of this gene is unknown. It is widely believed to be localized in the plasma membrane. The EMP3 protein is also conserved in a number of other proteins of the PMP22 family.
In adult humans, high levels of EMP3 are associated with poor prognosis. Its expression is regionally restricted and shows little cellular specificity. Studies of human brain organoids have also shown that the level of EMP3 is relatively low in the cortex and mesenchymal tissue. It is highly expressed in progenitor cells and mesenchymal cells. The results of these studies are promising in terms of predicting survival in patients with GBM.
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