Journal
JOURNAL OF CELL SCIENCE
Volume 121, Issue 24, Pages 4001-4007Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.036038
Keywords
DRMs; GPI-anchored proteins; Oligomerisation; Rafts; Sorting
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Funding
- Ministero dell'Universita e della Ricerca Scientifica e Tecnologica [FIRB 2004, PRIN 2006]
- ANR [05-BLAN 296-01]
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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.
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