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First published online September 29, 2004

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Rethinking rafts

Polarised epithelial cells generate their polarity by trafficking newly synthesised proteins to either the apical or basolateral plasma membrane. A long-standing hypothesis proposes that proteins are directed to the apical surface by associating with lipid rafts through glycosyl-phosphatidylinositol (GPI) anchors. Nigel Hooper and his colleagues challenge this dogma by showing that, in the case of porcine membrane dipeptidase (MDP), N-glycan sidechains rather than a GPI anchor direct apical targeting in kidney epithelial cells (see p. 5079). MDP contains a GPI anchor site and two N-glycosylation sites. The authors show that, although MDP lacking a GPI anchor site is secreted instead of being attached to the cell surface, it is still targeted to the apical surface. By contrast, when its N-glycosylation sites are removed, MDP localises to the basolateral membrane, even though it still associates with lipid rafts. Other proteins may use O-glycans instead of N-glycans as apical targeting signals, suggest the authors, and further studies should determine whether specific glycan sequences are required for targeting.

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Related articles in JCS:

N-Glycans, not the GPI anchor, mediate the apical targeting of a naturally glycosylated, GPI-anchored protein in polarised epithelial cells

Susan Pang, Paula Urquhart, and Nigel M. Hooper
JCS 2004 117: 5079-5086. [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?