Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein is a
protein that in humans is encoded by the PREX1gene.[5][6][7][8]
Function
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
The protein has been implicated in the spread of
melanoma skin cancer.[10]
Zhao T, Nalbant P, Hoshino M, et al. (April 2007). "Signaling requirements for translocation of P-Rex1, a key Rac2 exchange factor involved in chemoattractant-stimulated human neutrophil function". Journal of Leukocyte Biology. 81 (4): 1127–36.
doi:
10.1189/jlb.0406251.
PMID17227822.
S2CID25318452.
Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein is a
protein that in humans is encoded by the PREX1gene.[5][6][7][8]
Function
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
The protein has been implicated in the spread of
melanoma skin cancer.[10]
Zhao T, Nalbant P, Hoshino M, et al. (April 2007). "Signaling requirements for translocation of P-Rex1, a key Rac2 exchange factor involved in chemoattractant-stimulated human neutrophil function". Journal of Leukocyte Biology. 81 (4): 1127–36.
doi:
10.1189/jlb.0406251.
PMID17227822.
S2CID25318452.