The PX domain: a new phosphoinositide-binding module.

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.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

Ellson CD,Andrews S,Stephens LR,Hawkins PT

keywords:

subject

Has Abstract

pub_date

2002-03-15 00:00:00

pages

1099-105

issue

Pt 6

eissn

0021-9533

issn

1477-9137

journal_volume

115

pub_type

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