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PX domain

The PX domain is a phosphoinositide-binding structural domain involved in targeting of proteins to cell membranes.

This domain was first found in P40phox and p47phox domains of NADPH oxidase (phox stands for phagocytic oxidase). It was also identified in many other proteins involved in membrane trafficking, including nexins, Phospholipase D, and phosphoinositide-3-kinases.

The PX domain is structurally conserved in eukaryotes, although amino acid sequences show little similarity. PX domains interact primarily with PtdIns(3)P lipids. However some of them bind to phosphatidic acid, PtdIns(3,4)P2, PtdIns(3,5)P2, PtdIns(4,5)P2, and PtdIns(3,4,5)P3. The PX-domain can also interact with other domains and proteins.

Human proteins containing this domain

The human genome encodes about 40 PX-domain proteins, including multiple sorting nexins. Other examples include:

  • HS1BP3
  • KIF16B (SNX23)
  • NCF1; NCF1C; NCF4; NISCH
  • PIK3C2A; PIK3C2B; PIK3C2G; PLD1; PLD2; PXK
  • RPS6KC1
  • SGK3; SH3PXD2A; SNAG1; SNX9

References

References

  1. Ponting CP. (November 1996). "Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains?". Protein Sci..
  2. (June 2001). "Phoxy lipids: revealing PX domains as phosphoinositide binding modules". Cell.
  3. (June 2001). "Solution structure of the PX domain, a target of the SH3 domain". Nat. Struct. Biol..
  4. (October 2002). "Binding of the PX domain of p47phox to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction". EMBO J..
  5. (April 2003). "Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation". Proc. Natl. Acad. Sci. U.S.A..
  6. (November 2004). "The Phox Homology (PX) Domain Protein Interaction Network in Yeast". Molecular & Cellular Proteomics.
  7. (August 2001). "PX domains: attracted by phosphoinositides". Nature Cell Biology.
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