Different GPI-attachment signals affect the oligomerisation of GPI-anchored proteins and their apical sorting
| Autor: | Vincenza Campana, Simona Paladino, Chiara Zurzolo, Stéphanie Lebreton, Rosaria Tempre, Simona Tivodar |
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| Přispěvatelé: | Dipartimento di Biologia e Patologia Cellulare e Moleculare, University of Naples Federico II = Università degli studi di Napoli Federico II, CEINGE Biotecnologie Avanzate s.c.a.r.l., CEINGE - Biotecnologie Avanzate, Trafic membranaire et Pathogénèse, Institut Pasteur [Paris] (IP), Ministero dell'Università e della Ricerca Scientifica e Tecnologica (FIRB 2004, PRIN 2006), ANR-05-BLAN-0296,tri apical,Rôle des microdomaines lipidiques (ou rafts) dans les mécanismes d'adressage apical des protéines glypiées (protéines GPI) dans les cellules épithéliales(2005), Università degli studi di Napoli Federico II, Institut Pasteur [Paris], Paladino, Simona, Lebreton, S., Tivodar, S., Campana, V., Tempre, R., Zurzolo, Chiara |
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Glycosylphosphatidylinositols
Prions Recombinant Fusion Proteins Green Fluorescent Proteins Receptors Cell Surface [SDV.BC]Life Sciences [q-bio]/Cellular Biology Biology Green fluorescent protein Cell Line 03 medical and health sciences 0302 clinical medicine Dogs Animals Receptor Raft 030304 developmental biology 0303 health sciences GPI-anchored protein Sorting Folate Receptors GPI-Anchored Oligomerisation Membrane Proteins Epithelial Cells Cell Biology Fusion protein Gpi anchored protein Transport protein Cell biology carbohydrates (lipids) Protein Transport Cholesterol DRM Apical sorting Cell culture Folate receptor lipids (amino acids peptides and proteins) Carrier Proteins 030217 neurology & neurosurgery |
| Zdroj: | Journal of Cell Science Journal of Cell Science, 2008, 121(Pt 24), pp.4001-7. ⟨10.1242/jcs.036038⟩ Journal of Cell Science, Company of Biologists, 2008, 121(Pt 24), pp.4001-7. ⟨10.1242/jcs.036038⟩ |
| ISSN: | 0021-9533 1477-9137 |
| DOI: | 10.1242/jcs.036038⟩ |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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