The PX domain: a new phosphoinositide-binding module.

  • Ellson C
  • Andrews S
  • Stephens L
 et al. 
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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.

Author-supplied keywords

  • Binding Sites
  • Carrier Proteins
  • Endosomes
  • Eye Proteins
  • Fatty Acid-Binding Proteins
  • Models
  • Molecular
  • Phagosomes
  • Phosphatidylinositol Phosphates
  • Phosphatidylinositols
  • Protein Structure
  • Tertiary
  • Vacuoles
  • src Homology Domains

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Authors

  • Chris D Ellson

  • Simon Andrews

  • Len R Stephens

  • Phill T Hawkins

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