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First published online December 3, 2008
doi: 10.1242/10.1242/jcs.036038

Journal of Cell Science 121, 4001-4007 (2008)
Published by The Company of Biologists 2008
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Short Report

Different GPI-attachment signals affect the oligomerisation of GPI-anchored proteins and their apical sorting

Simona Paladino1,2, Stephanie Lebreton3, Simona Tivodar1, Vincenza Campana3, Rosaria Tempre1 and Chiara Zurzolo1,3,*

1 Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università degli Studi di Napoli Federico II
2 CEINGE Biotecnologie Avanzate Scarl, via S. Pansini 5, 80131 Napoli, Italy
3 Unité de Trafic Membranaire et Pathogénèse, Institut Pasteur, 25 rue du Docteur Roux, Paris 75724, France

* Author for correspondence (e-mail: zurzolo{at}pasteur.fr; zurzolo{at}unina.it)

Accepted 18 September 2008

Summary

To understand the mechanism involved in the apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) we fused to the C-terminus of GFP the GPI-anchor-attachment signal of the folate receptor (FR) or of the prion protein (PrP), two native GPI-anchored proteins that are sorted apically or basolaterally, respectively, in MDCK cells. We investigated the behaviour of the resulting fusion proteins GFP-FR and GFP-PrP by analysing three parameters: their association with DRMs, their oligomerisation and their apical sorting. Strikingly, we found that different GPI-attachment signals differently modulate the ability of the resulting GFP-fusion protein to oligomerise and to be apically sorted. This is probably owing to differences in the GPI anchor and/or in the surrounding lipid microenvironment. Accordingly, we show that addition of cholesterol to the cells is necessary and sufficient to drive the oligomerisation and consequent apical sorting of GFP-PrP, which under control conditions does not oligomerise and is basolaterally sorted.

Key words: DRMs, GPI-anchored proteins, Oligomerisation, Rafts, Sorting






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