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Gene Review

PREX1  -  phosphatidylinositol-3,4,5-trisphosphate...

Homo sapiens

Synonyms: KIAA1415, P-REX1, P-Rex1, Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein, PtdIns(3,4,5)-dependent Rac exchanger 1
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Disease relevance of PREX1


High impact information on PREX1

  • P-Rex1 appears to be a coincidence detector in PtdIns(3,4,5)P3 and Gbetagamma signaling pathways that is particularly adapted to function downstream of heterotrimeric G proteins in neutrophils [2].
  • P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac [2].
  • Phosphorylation of P-Rex1 by the cyclic AMP-dependent protein kinase inhibits the phosphatidylinositiol (3,4,5)-trisphosphate and Gbetagamma-mediated regulation of its activity [3].
  • Treatment with isoproterenol or S(p)-cAMPS, a potent activator of PKA, increased the incorporation of (32)P into P-Rex1 [3].
  • Deletion of the DEP, PDZ, or inositol polyphosphate 4-phosphatase homology domains has no major consequences on the abilities of either PtdIns(3,4,5)P3 or Gbetagamma subunits to stimulate P-Rex1 Rac-GEF activity [4].

Biological context of PREX1

  • We have investigated here the mechanisms of stimulation of P-Rex1 Rac-GEF activity by the lipid second messenger phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3) and the Gbetagamma subunits of heterotrimeric G proteins [4].
  • Redistribution of P-Rex1 to the leading edge was also dependent on tyrosine kinase activity and was modulated by cell adhesion [5].
  • As a selective catalyst for Rac2 activation, P-Rex1 serves as an important regulator of human neutrophil NADPH oxidase activity and chemotaxis in response to a variety of extracellular stimuli [5].
  • P-Rex2 has structure, activity and regulatory properties similar to P-Rex1 but has divergent tissue distribution, as P-Rex1 is mainly expressed in neutrophils [6].
  • PREX is a positive regulatory element for xenobiotic responsive element (XRE)-mediated gene expression that is located upstream of the XRE in the CYP2A8 gene [7].

Anatomical context of PREX1

  • PI 3,4,5-trisphosphate [PI(3,4,5)P(3); PIP(3)]-dependent Rac exchanger 1 (P-Rex1) is a Rac-specific guanine nucleotide exchange factor abundant in neutrophils and myeloid cells [5].
  • The exchange activity of P-Rex1 is synergistically activated by the binding of PIP(3)and betagamma subunits of heterotrimeric G proteins in vitro, suggesting that the association of P-Rex1 with membranes is a prerequisite for cellular activation [5].

Associations of PREX1 with chemical compounds


Other interactions of PREX1

  • However, the spatial regulation of endogenous P-Rex1 has not been well defined, particularly in human neutrophils activated through G protein-coupled receptors [5].
  • P-Rex1 is mainly expressed in neutrophils and regulates reactive oxygen species formation in these cells (Welch et al., 2002), whereas P-Rex2 is expressed in a wide variety of tissues but not in neutrophils (Donald et al., 2004), and P-Rex2B is expressed in the heart (Rosenfeldt et al., 2004) [8].

Analytical, diagnostic and therapeutic context of PREX1

  • In situ hybridization revealed that P-Rex1 is dynamically expressed in a variety of cells in the developing mouse brain, including some cortical and DRG neurons [1].


  1. Involvement of a Rac activator,P-Rex1, in neurotrophin-derived signaling and neuronal migration. Yoshizawa, M., Kawauchi, T., Sone, M., Nishimura, Y.V., Terao, M., Chihama, K., Nabeshima, Y., Hoshino, M. J. Neurosci. (2005) [Pubmed]
  2. P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac. Welch, H.C., Coadwell, W.J., Ellson, C.D., Ferguson, G.J., Andrews, S.R., Erdjument-Bromage, H., Tempst, P., Hawkins, P.T., Stephens, L.R. Cell (2002) [Pubmed]
  3. Phosphorylation of P-Rex1 by the cyclic AMP-dependent protein kinase inhibits the phosphatidylinositiol (3,4,5)-trisphosphate and Gbetagamma-mediated regulation of its activity. Mayeenuddin, L.H., Garrison, J.C. J. Biol. Chem. (2006) [Pubmed]
  4. Regulation of P-Rex1 by phosphatidylinositol (3,4,5)-trisphosphate and Gbetagamma subunits. Hill, K., Krugmann, S., Andrews, S.R., Coadwell, W.J., Finan, P., Welch, H.C., Hawkins, P.T., Stephens, L.R. J. Biol. Chem. (2005) [Pubmed]
  5. Signaling requirements for translocation of P-Rex1, a key Rac2 exchange factor involved in chemoattractant-stimulated human neutrophil function. Zhao, T., Nalbant, P., Hoshino, M., Dong, X., Wu, D., Bokoch, G.M. J. Leukoc. Biol. (2007) [Pubmed]
  6. P-Rex2, a new guanine-nucleotide exchange factor for Rac. Donald, S., Hill, K., Lecureuil, C., Barnouin, R., Krugmann, S., John Coadwell, W., Andrews, S.R., Walker, S.A., Hawkins, P.T., Stephens, L.R., Welch, H.C. FEBS Lett. (2004) [Pubmed]
  7. Transcription factor NF2d9 (LBP-1a) interacts with the positive regulatory element for the xenobiotic responsive element. Kurose, K., Tohkin, M., Hasegawa, R. Biochim. Biophys. Acta (2005) [Pubmed]
  8. Purification of P-Rex1 from neutrophils and nucleotide exchange assay. Hill, K., Welch, H.C. Meth. Enzymol. (2006) [Pubmed]
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