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| The EMBO Journal
(2001) 20, 5863–5875, doi:10.1093/emboj/20.21.5863 |
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| The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein |
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| Sabine Gauczynski1, 3, Jean-Michel Peyrin2, 3, Stéphane Haïk2, 3, Christoph Leucht1, Christoph Hundt1, Roman Rieger1, Susanne Krasemann1, Jean-Philippe Deslys2, Dominique Dormont2, Corinne Ida Lasmézas1, 2, 4 and Stefan Weiss1, 4 |
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1 Laboratorium für Molekulare Biologie-Genzentrum-Institut für Biochemie der LMU München, Feodor-Lynen Str. 25, D-81377 Munich, Germany 2 CEA, Service de Neurovirologie, DRM/DSV, CRSSA, 18, Route du Panorama, BP.6, F-92265, Fontenay-aux-Roses Cedex, France 3 S.Gauczynski, J.-M.Peyrin and S.Haïk contributed equally to this work 4 C.I.Lasmézas and S.Weiss should be considered as the senior authors of this work To whom correspondence should be addressed Corinne Ida Lasmézas, corinne.lasmezas@cea.fr Stefan Weiss, Weiss@lmb.uni-muenchen.de Received 14 November 2000; Revised 9 August 2001; Accepted 5 September 2001. |
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| Abstract |
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| Recently, we identified the 37-kDa laminin receptor precursor (LRP) as an interactor for the prion protein (PrP). Here, we show the presence of the 37-kDa LRP and its mature 67-kDa form termed high-affinity laminin receptor (LR) in plasma membrane fractions of N2a cells, whereas only the 37-kDa LRP was detected in baby hamster kidney (BHK) cells. PrP co-localizes with LRP/LR on the surface of N2a cells and Semliki Forest virus (SFV) RNA transfected BHK cells. Cell-binding assays reveal the LRP/LR-dependent binding of cellular PrP by neuronal and non-neuronal cells. Hyperexpression of LRP on the surface of BHK cells results in the binding of exogenous PrP. Cell binding is similar in PrP+/+ and PrP0/0 primary neurons, demonstrating that PrP does not act as a co-receptor of LRP/LR. LRP/LR-dependent internalization of PrP is blocked at 4°C. Secretion of an LRP mutant lacking the transmembrane domain (aa 86–101) from BHK cells abolishes PrP binding and internalization. Our results show that LRP/LR acts as the receptor for cellular PrP on the surface of mammalian cells. |
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| Keywords: 37-kDa laminin receptor precursor, 67-kDa high-affinity laminin receptor, prion receptor, PrP internalization, Semliki Forest virus |
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