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Commentary |
1 The Inositide Laboratory, The Babraham Institute, Babraham, Cambridge, CB2
4AT, UK
2 Bioinformatics, The Babraham Institute, Babraham, Cambridge, CB2 4AT, UK
* Author for correspondence (e-mail: chris.ellson{at}bbsrc.ac.uk )
The PX domain, which until recently was an orphan domain, has emerged as the latest member of the phosphoinositide-binding module superfamily. Structural studies have revealed that it has a novel fold and identified key residues that interact with the bound phosphoinositide, enabling some prediction of phosphoinositide-binding specificity. Specificity for PtdIns(3)P appears to be the most common, and several proteins containing PX domains localise to PtdIns(3)P-rich endosomal and vacuolar structures through their PX domains: these include the yeast t-SNARE Vam7p, mammalian sorting nexins (involved in membrane trafficking events) and the Ser/Thr kinase CISK, which is implicated in cell survival. Additionally, phosphoinositide binding to the PX domains of p40phox and p47phox appears to play a critical role in the active assembly of the neutrophil oxidase complex.
Key words: Phox, PI3-kinase, PtdIns(3)P, Trafficking, NADPH oxidase, SNX
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