Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein is a protein that in humans is encoded by the PREX1 gene.[5][6][7][8]

PREX1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPREX1, P-REX1, phosphatidylinositol-3,4,5-trisphosphate dependent Rac exchange factor 1
External IDsOMIM: 606905 MGI: 3040696 HomoloGene: 10821 GeneCards: PREX1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_020820

NM_177782

RefSeq (protein)

NP_065871

NP_808450

Location (UCSC)Chr 20: 48.62 – 48.83 MbChr 2: 166.41 – 166.56 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function edit

The protein encoded by this gene acts as a guanine nucleotide exchange factor for the RHO family of small GTP-binding proteins (RACs). It has been shown to bind to and activate RAC1 by exchanging bound GDP for free GTP. The encoded protein, which is found mainly in the cytoplasm, is activated by phosphatidylinositol-3,4,5-trisphosphate and the beta-gamma subunits of heterotrimeric G proteins.[8] The activation of P-REX1 is efficient when chemotactic receptors coupled to Gi proteins are activated, as a consequence of a better release of the Gβɣ heterodimer.[9]

Clinical significance edit

The protein has been implicated in the spread of melanoma skin cancer.[10]

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000124126Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000039621Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Welch HC, Coadwell WJ, Ellson CD, et al. (March 2002). "P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac". Cell. 108 (6): 809–21. doi:10.1016/S0092-8674(02)00663-3. PMID 11955434. S2CID 14185057.
  6. ^ Hill K, Krugmann S, Andrews SR, et al. (February 2005). "Regulation of P-Rex1 by phosphatidylinositol (3,4,5)-trisphosphate and Gbetagamma subunits". The Journal of Biological Chemistry. 280 (6): 4166–73. doi:10.1074/jbc.M411262200. PMID 15545267.
  7. ^ Mayeenuddin LH, Garrison JC (January 2006). "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". The Journal of Biological Chemistry. 281 (4): 1921–8. doi:10.1074/jbc.M506035200. PMID 16301320.
  8. ^ a b "Entrez Gene: PREX1 phosphatidylinositol 3,4,5-trisphosphate-dependent RAC exchanger 1".
  9. ^ Cervantes-Villagrana RD, Adame-García SR, García-Jiménez I, et al. (January 2019). "13 proteins". The Journal of Biological Chemistry. 294 (2): 531–546. doi:10.1074/jbc.RA118.006254. PMC 6333895. PMID 30446620.
  10. ^ Lindsay CR, Lawn S, Campbell AD, et al. (November 2011). "P-Rex1 is required for efficient melanoblast migration and melanoma metastasis". Nature Communications. 2: 555. Bibcode:2011NatCo...2..555L. doi:10.1038/ncomms1560. PMC 3400057. PMID 22109529.

Further reading edit