Regular ArticleAssignment of O-Glycan Attachment Sites to the Hinge-like Regions of Human Lysosomal Membrane Glycoproteins Lamp-1 and Lamp-2
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The two-domain architecture of LAMP2A regulates its interaction with Hsc70
2022, Experimental Cell ResearchCitation Excerpt :Previously, we proposed that the linker regions are perpendicular to the membrane along the C-domains [18]. The linker regions are expected to be elongated and rigid after O-glycosylation [35]. With this model, the presence of the linker regions can explain the steric hindrance of AlocLys at the edge of side A and the occupation of pBpa in the central part, by forming the cavity between the two LAMP2A molecules (Fig. S5B).
LAMP-1-chimeric DNA vaccines enhance the antibody response in Japanese flounder, Paralichthys olivaceus
2017, Fish and Shellfish ImmunologyMelanoma cell galectin-1 ligands functionally correlate with malignant potential
2015, Journal of Investigative DermatologyLysosome-associated membrane proteins (LAMPs) regulate intracellular positioning of mitochondria in MC3T3-E1 cells
2015, Experimental Cell ResearchCitation Excerpt :Although mouse LAMP-1 and LAMP-2 are composed of 406 and 415 amino acid residues, respectively, LAMP-1 migrated much faster than LAMP-2 after the N-glycosylation removal. This can be explained by the fact that LAMP-2 has more O-linked glycosylation sites in the linker region between the two domains than LAMP-1, in the case of the human proteins [24]. After the treatment with the LAMP-2 siRNA, the amount of LAMP-2 was appreciably decreased (Fig. 3B), without affecting LAMP-1 expression, indicating that the siRNA acted specifically on LAMP-2.
Pompe disease results in a Golgi-based glycosylation deficit in human induced pluripotent stem cell-derived cardiomyocytes
2015, Journal of Biological ChemistryCitation Excerpt :We decided to investigate the cause for the differences in mobility of the LAMPs in the Pompe iPSC-CMs by focusing on glycosylation, as both of these proteins are heavily glycosylated by traditional N- and O-linked endoplasmic reticulum (ER)-to-Golgi glycan biosynthesis pathways. In addition, several of the N-linked adducts are modified by long poly-N-acetyllactosamines added in the Golgi apparatus (38–41). To test the hypothesis that a deficit in Golgi-based glycosylation is the source of lower molecular weight LAMP species, iPSC-CMs were exposed to brefeldin A (BFA), a fungal metabolite that causes collapse of the Golgi stacks, disrupting Golgi-based glycosylation (42).