P-Rex1 and P-Rex2 RacGEFs and cancer

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Nuthasuda Srijakotre1, Joey Man1, Lisa M Ooms1

  • 1Cancer Program, Monash Biomedicine Discovery Institute, and Department of Biochemistry and Molecular Biology, Monash University, 23 Innovation Walk, Clayton, VIC 3800, Australia.

Biochemical Society Transactions
|July 16, 2017
PubMed

Insights

Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchangers (P-Rex1 and P-Rex2) show oncogenic roles in cancers. Their altered expression and mutation impact tumor outcomes, especially in breast cancer and melanoma.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • P-Rex proteins are RacGEFs activated by phosphatidylinositol 3,4,5-trisphosphate and Gβγ subunits.
  • P-Rex1 and P-Rex2 share structural and functional similarities.
  • Both P-Rex proteins are implicated in human cancer development.

Purpose of the Study:

  • To compare the functions of P-Rex1 and P-Rex2 in human cancers.
  • To elucidate their cellular effects and signaling mechanisms in oncogenesis.
  • To review emerging clinical data on their impact on tumor outcomes.

Main Methods:

  • Comparative analysis of P-Rex1 and P-Rex2 functions.
  • Review of existing literature on P-Rex proteins in cancer.
  • Examination of cellular effects and signaling pathways.

Main Results:

  • P-Rex1 and P-Rex2 exhibit oncogenic roles, with P-Rex1 often overexpressed and P-Rex2 mutated in cancers.
  • Alterations in P-Rex1 and P-Rex2 are observed in breast cancer, prostate cancer, and melanoma.
  • Functional similarities and differences between P-Rex1 and P-Rex2 in cancer contexts were detailed.

Conclusions:

  • P-Rex1 and P-Rex2 are significant players in human oncogenesis.
  • Changes in P-Rex1 and P-Rex2 expression or mutation are linked to tumor progression.
  • Further research into P-Rex proteins may offer new therapeutic strategies for cancer.
Keywords:
PREX1PREX2RacGEFcancer

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