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First published online November 3, 2003

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p24 proteins - masters of their domains

The p24 proteins (p23, p24, p25 and p26) are an enigmatic family of transmembrane proteins that function early in the secretory pathway, localizing primarily to the Golgi. Their precise roles are controversial, partly because it is difficult to study proteins that both heterooligomerize and cycle between different membrane compartments. Jean Gruenberg and co-workers have got round the problem by generating a p25 mutant (p25SS) that lacks the normal KKXX ER-retrieval signal - the mutant escapes from the early secretory pathway, allowing examination of its behaviour in membranes that normally lack p24 proteins (see p. 4821). The authors observe that, in the presence of p25SS, other p24 proteins also escape the early secretory pathway, suggesting that p25 normally anchors them there. Combining advanced confocal microscopy and immunoelectron microscopy, they then demonstrate that p25SS ends up in late endosomes, in which it is confined to discrete membrane domains and interferes with cholesterol distribution. The p25SS domains are distinct from lipid rafts, exclude other transmembrane proteins and probably represent higher-order oligomers. Given this ability to exclude cholesterol, p25 could play an important role defining Golgi membrane domains and modulating their dynamics.

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Related articles in JCS:

The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics

Gregory Emery, Robert G. Parton, Manuel Rojo, and Jean Gruenberg
JCS 2003 116: 4821-4832. [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?