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Originally published In Press as doi:10.1074/jbc.M203661200 on June 17, 2002

J. Biol. Chem., Vol. 277, Issue 36, 33311-33318, September 6, 2002
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Endocytic Intermediates Involved with the Intracellular Trafficking of a Fluorescent Cellular Prion Protein*

Ana C. Magalhãesabc, Juliana A. Silvaabd, Kil S. Leeefg, Vilma R. Martinse, Vania F. Pradoh, Stephen S. G. Fergusoni, Marcus V. Gomeza, Ricardo R. Brentanie, and Marco A. M. Pradoaj

From the a Laboratório de Neurofarmacologia, Departamento de Farmacologia and the h Departamento de Bioquímica-Imunologia, ICB, Universidade Federal de Minas Gerais, Belo Horizonte, Minas Gerais 31270-910, Brazil, the e Ludwig Institute for Cancer Research, São Paulo Branch, Rua Antonio Prudente 109/4A, São Paulo 01509-010 SP, Brazil, the f Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo 01509-010, Brazil, and the i J. P. Robarts Research Institute and Department of Physiology, University of Western Ontario, 100 Perth Dr., P. O. Box 5015, London, Ontario N6A 5K8, Canada

We have investigated the intracellular traffic of PrPc, a glycosylphosphatidylinositol (GPI)-anchored protein implicated in spongiform encephalopathies. A fluorescent functional green fluorescent protein (GFP)-tagged version of PrPc is found at the cell surface and in intracellular compartments in SN56 cells. Confocal microscopy and organelle-specific markers suggest that the protein is found in both the Golgi and the recycling endosomal compartment. Perturbation of endocytosis with a dynamin I-K44A dominant-negative mutant altered the steady-state distribution of the GFP-PrPc, leading to the accumulation of fluorescence in unfissioned endocytic intermediates. These pre-endocytic intermediates did not seem to accumulate GFP-GPI, a minimum GPI-anchored protein, suggesting that PrPc trafficking does not depend solely on the GPI anchor. We found that internalized GFP-PrPc accumulates in Rab5-positive endosomes and that a Rab5 mutant alters the steady-state distribution of GFP-PrPc but not that of GFP-GPI between the plasma membrane and early endosomes. Therefore, we conclude that PrPc internalizes via a dynamin-dependent endocytic pathway and that the protein is targeted to the recycling endosomal compartment via Rab5-positive early endosomes. These observations indicate that traffic of GFP-PrPc is not determined predominantly by the GPI anchor and that, different from other GPI-anchored proteins, PrPc is delivered to classic endosomes after internalization.

* This work was supported in part by Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Grant 99/07124-8 (to V. R. M.), Pronex, Programa de Apoio ao Desenvolvimento Científico e Tecnológico (PADCT), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), and Fundação de Amparo à Pesquisa de Minas Gerais (FAPEMIG) (to A. M. P.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

b Both authors contributed equally to this work.

c Received a Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Ph.D. fellowship.

d Supported by a CNPq Post-doctoral fellowship.

g Received a Ph.D. fellowship from FAPESP (00/03629-7).

j To whom correspondence should be addressed: Laboratório de Neurofarmacologia, Departamento de Farmacologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Av. Antonio Carlos 6627, Belo Horizonte, Minas Gerais 31270-910, Brazil. Tel.: 55-31-3499-2718; Fax: 55-31-3499-2695; E-mail: mprado@icb.ufmg.br.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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