Plasmolipin is a protein encoded by the PLLP gene in humans. The PLLP is localized and recycled between the serosa and the Golgi. In the Golgi apparatus, PLLP forms an oligomer based on fluorescence resonance energy transfer (annoyance) analysis. Golgi entering the plasma membrane transport of the secreted protein vesicular stomatitis virus G protein (VSVG), rather than a VSVG mutant with an elongated transmembrane domain is stopped by PLLP. Laurdan staining analysis indicated that the block was associated with pllp-induced proliferation of the membrane.
|Basic Information of PLLP|
|Aliases||Plasma membrane proteolipid|
|Organism||Homo sapiens (Human)|
Plasmolipin (PLLP) contains a protein-related flux in the vesicle-associated domain and is highly expressed in the brain associated with myelin-associated regions, but also in the apical region of epithelial cells. Myelin constitutes a compact stack of large surface areas, a protein-poor thick film that isolates axons to allow for rapid signal transmission. The increase in PLLP is involved in postpartum myelination, but its function remains unknown. In the primary glial and cultured cells, fluorescently labeled PLLP and antibodies were used against PLLP, and their intracellular localization and kinetic properties were significant. Previous studies have shown that in the Golgi apparatus, PLLP aggregates potential myelin membrane precursor domains through its oligomerization and liquid-attracting lipids. These data support a model in which PLLP acts as a myelin through the tissue myelin lining membrane.
Fig.1 The structure of Plasmolipin.
The authors identified a new participant, a protein that was previously uncharacteristically called Plasmolipin. Not only did they report the mechanism of action through binding to epsin, but they also emphasized the important role of Notch signaling in controlling epithelial cell differentiation.
These results indicate that PLLP is an effective receptor for McERV.
These results indicate that methylation of the CRMP4 gene in PLLP is significantly increased, suggesting its potential of being a new predictor of PLLP.
These results show that PLLP expression induces apical debris (Crb) internalization and activation of the Notch signaling pathway, both of which are key steps in obtaining cell polarity and epithelial cell differentiation.
These data support a model in which PLLP exerts myelin action through the tissue myelin liquid membrane.
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