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Publication : Subcellular localization of prion proteins and the 37 kDa/67 kDa laminin receptor fused to fluorescent proteins.

First Author  Nikles D Year  2008
Journal  Biochim Biophys Acta Volume  1782
Issue  5 Pages  335-40
PubMed ID  18339329 Mgi Jnum  J:136730
Mgi Id  MGI:3796913 Doi  10.1016/j.bbadis.2008.02.003
Citation  Nikles D, et al. (2008) Subcellular localization of prion proteins and the 37 kDa/67 kDa laminin receptor fused to fluorescent proteins. Biochim Biophys Acta 1782(5):335-40
abstractText  The 37 kDa/67 kDa laminin receptor LRP/LR acts as a receptor for both PrPc and PrPSc at the cell surface. Here, we further analyzed the subcellular localization of fluorescent labeled prion protein (PrP) and laminin receptor (LRP/LR) molecules. We show that EGFP-PrP is localized at the cell surface and in a perinuclear compartment, respectively. In contrast, a DsRed-DeltaSP-PrP mutant lacking the signal peptide is almost exclusively found in the nucleus but does not colocalize with heterochromatin. Interestingly, LRP-DsRed efficiently colocalizes with EGFP-PrP in the perinuclear compartment and LRP-ECFP partly colocalizes with DsRed-DeltaSP-PrP in the nucleus, respectively. We conclude that the interactions of PrP and LRP/LR are not restricted to the cell surface but occur also in intracellular compartments suggesting a putative role of LRP/LR in the trafficking of PrP molecules.
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