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Lysosome-associated membrane protein 2 (LAMP 2), also known as lgp2 or lgp110, is a type 1 integral membrane protein that is transported from the trans-Golgi network to endosomes and then lysosomes. LAMPs, also known as lysosomal integral membrane proteins (LIMPs), are ubiquitous, highly glycosylated and account for ~50% of lysosomal membrane protein; their function is largely unknown. All LAMPs have a short, 10-20 amino acid, cytosolic domain which contain single tyrosine or di-leucine motifs, that interact with adaptor complexes (APS) for sorting at the trans-Golgi network and targeting to lysosomes. LAMP 2 has also been detected at the plasma membrane of cells in a differentiation and activation dependant manner, as well as in cells that secrete lysosomal hydrolases. A study in the developmental expression patterns of membrane LAMP 2 transcripts indicate a possible involvement of this protein in cell-cell or cell-extracellular matrix interaction, and appear to reflect tissue and cell type specific roles of lysosomes during morphogenesis. Cell surface LAMP 1 and 2 have been shown to promote adhesion of human peripheral blood mononuclear cells (PBMC) to vascular endothelium, possibly involved in the adhesion of PBMC to the site of inflammation. Studies with LAMP 2 deficient mice indicate LAMP 2 is critical for autophagy, in conversion of early autophagic vacuoles to vacuoles, which rapidly degrade their content. It is also the primary defect in Danon disease. The trans-Golgi network (TGN) is part of the secretory pathway of eukaryotic cells which is distinct from the Golgi stack. The TGN is important in the later stages of protein secretion where it seems to play a key role in the sorting and targeting of secreted proteins to the correct destination. Some surface receptors recycle between the cell surface and the TGN, suggesting that the TGN is also important in endocytic pathways.


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