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

Abstract:

: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.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

Paladino S,Lebreton S,Tivodar S,Campana V,Tempre R,Zurzolo C

doi

10.1242/jcs.036038

subject

Has Abstract

pub_date

2008-12-15 00:00:00

pages

4001-7

issue

Pt 24

eissn

0021-9533

issn

1477-9137

pii

121/24/4001

journal_volume

121

pub_type

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