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PLP2 encodes an integral membrane protein that localizes to the endoplasmic reticulum in colonic epithelial cells.
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PLP2 specifically binds to phosphatidylinositol 3 kinase to activate the protein kinase B (show AKT1 Proteins) pathway to enhance cell proliferation, adhesion, and invasion in melanoma cells.
miR (show MLXIP Proteins)-664 negatively regulates PLP2 and promotes proliferation and invasion of T-ALL cell lines. Thus, miR (show MLXIP Proteins)-664 may represent a potential therapeutic target for T-ALL intervention.
PLP2 and RAB5C are binding partners of TPD52.
This work ascribes a critical function to PLP2 for viral ligase activity and underlines the power of non-lethal haploid genetic screens in human cells to identify the genes involved in pathogen manipulation of the host immune system.
PLP2/A4 has a role in the chemotactic processes via CCR1
PLP2 is expressed abundantly in the pyramidal cells of hippocampus and granular cells of the cerebellum in the brains of a cohort of males with probable X-linked mental retardation.
PLP2 enhanced proliferation, adhesion, invasion, and MMP-2 (show MMP2 Proteins) secretion in vitro, and tumor metastasis in vivo.
This gene encodes an integral membrane protein that localizes to the endoplasmic reticulum in colonic epithelial cells. The encoded protein can multimerize and may function as an ion channel. A polymorphism in the promoter of this gene may be linked to an increased risk of X-linked mental retardation. A pseudogene of this gene is found on chromosome 5.
A4 differentiation-dependent protein
, differentiation-dependent protein A4
, intestinal membrane A4 protein
, proteolipid protein 2
, Proteolipid protein 2 (intestinal membrane A4 protein)
, proteolipid protein 2 (colonic epithelium-enriched) S homeolog
, proteolipid protein 2 S homeolog