Subcellular localization of prion proteins and the 37 kDa/67 kDa laminin receptor fused to fluorescent proteins.
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.
Nikles
Daphne
D
Laboratorium für Molekulare Biologie - Genzentrum-Institut für Biochemie der LMU München, Feodor-Lynen-Str. 25, 81377 München, Germany.
Vana
Karen
K
Gauczynski
Sabine
S
Knetsch
Heike
H
Ludewigs
Heike
H
Weiss
Stefan
S
D000818:Animals; D002451:Cell Compartmentation; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism; D003001:Cloning, Molecular; D006570:Heterochromatin / Q000378:metabolism; D008164:Luminescent Proteins / Q000378:metabolism*; D051379:Mice; D008970:Molecular Weight; D050505:Mutant Proteins / Q000378:metabolism; D011328:Prions / Q000378:metabolism*; D021381:Protein Transport; D017474:Receptors, Laminin / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism*; D013347:Subcellular Fractions / Q000378:metabolism
D006570:Heterochromatin; D008164:Luminescent Proteins; D050505:Mutant Proteins; D011328:Prions; D017474:Receptors, Laminin; D011993:Recombinant Fusion Proteins