The PX domain: a new phosphoinositide-binding module
Author:
Ellson Chris D.1, Andrews Simon2, Stephens Len R.1, Hawkins Phill T.1
Affiliation:
1. The Inositide Laboratory, The Babraham Institute, Babraham, Cambridge, CB2 4AT, UK 2. Bioinformatics, The Babraham Institute, Babraham, Cambridge, CB2 4AT, UK
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 p40phox and p47phox appears to play a critical role in the active assembly of the neutrophil oxidase complex.
Publisher
The Company of Biologists
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