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The PX domain

The wide-ranging cellular effects of phosphoinositides are mediated through their interaction with proteins containing lipid-binding modules such as pleckstrin homology and FYVE domains. Recent work has revealed that the PX domain — a domain first identified in NADPH oxidase subunits several years ago — is also a phosphoinositide-binding module. On p. 1099, Chris Ellson and co-workers discuss studies that are shedding light on the structure and function of this domain, which in most cases is specific for PtdIns(3)P. NMR and X-ray crystallography have revealed that the PX domain has a novel `wedge-like' fold in which one face forms the phosphoinositide-binding pocket; these studies are also beginning to establish the residues that determine ligand binding specificity. The domain is most common in proteins involved in membrane trafficking — for example, the t-SNARE Vam7p and sorting nexins. It appears to target these proteins to PtdIns(3)P-rich membranes. The latter include endosomes and vacuoles, in which PtdIns(3)P levels do not vary, as well as phagosomes, in which PtdIns(3)P levels are regulated by external stimuli.

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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 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?