J Cell Sci. 2002 Mar 15;115(Pt 6):1099-105.

The PX domain: a new phosphoinositide-binding module.

Ellson CD, Andrews S, Stephens LR, Hawkins PT.

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The Inositide Laboratory, The Babraham Institute, Babraham, Cambridge, CB2 4AT, UK. chris.ellson@bbsrc.ac.uk

Erratum in

J Cell Sci 2002 May 1;115(Pt 9):1995.

Abstract

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 p40(phox) and p47(phox) appears to play a critical role in the active assembly of the neutrophil oxidase complex.

PMID:: 11884510; [PubMed - indexed for MEDLINE]

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