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First published online March 7, 2007

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Transmembrane proteins sorted!

In epithelial cells, sorting of glycosylphosphatidylinositol-anchored proteins to the apical surface requires their interaction with lipid rafts – Triton-X-100-resistant membrane microdomains. Apical transmembrane proteins, although insoluble in weaker detergents such as Lubrol, tend to be soluble in Triton X-100. So are detergent-resistant rafts important for sorting of these proteins? On p. 1009, Jean-Louis Delaunay and colleagues report that for nucleotide pyrophosphatases/phosphodiesterases (NPPases), type II transmembrane proteins, there is not a strict correlation between detergent resistance and apical targeting. NPP1 is basolaterally localised and detergent soluble, whereas NPP3 is apically localised and Lubrol-insoluble. To examine the relationship between detergent resistance and apical targeting of these proteins, the authors stably transfected MDCK cells with wild-type NPP1 and NPP3, tail mutants, and chimeric constructs that combined different domains of the two proteins. Their results indicate that Lubrol resistance is an intrinsic property of NPP3 that does not determine its final destination. This is therefore strong evidence against the theory that Lubrol-resistant rafts target NPP3 and other transmembrane proteins to the apical membrane.

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Related articles in JCS:

Differential detergent resistance of the apical and basolateral NPPases: relationship with polarized targeting

Jean-Louis Delaunay, Michelyne Breton, James W. Goding, Germain Trugnan, and Michèle Maurice
JCS 2007 120: 1009-1016. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?