| First Author | Ellson CD | Year | 2002 |
| Journal | J Cell Sci | Volume | 115 |
| Issue | Pt 6 | Pages | 1099-105 |
| PubMed ID | 11884510 | Mgi Jnum | J:75847 |
| Mgi Id | MGI:2177922 | Doi | 10.1242/jcs.115.6.1099 |
| Citation | Ellson CD, et al. (2002) The PX domain: a new phosphoinositide-binding module. J Cell Sci 115(Pt 6):1099-105 |
| abstractText | 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. |
