Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger (P-Rex) proteins are RacGEFs that are synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and Gβγ subunits of G-protein-coupled receptors. P-Rex1 and P-Rex2 share similar amino acid sequence homology, domain structure, and catalytic function. Recent evidence suggests that both P-Rex proteins may play oncogenic roles in human cancers. P-Rex1 and P-Rex2 are altered predominantly via overexpression and mutation, respectively, in various cancer types, including breast cancer, prostate cancer, and melanoma. This review compares the similarities and differences between P-Rex1 and P-Rex2 functions in human cancers in terms of cellular effects and signalling mechanisms. Emerging clinical data predict that changes in expression or mutation of P-Rex1 and P-Rex2 may lead to changes in tumour outcome, particularly in breast cancer and melanoma.
P-Rex1 and P-Rex2 RacGEFs and cancer
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Nuthasuda Srijakotre, Joey Man, Lisa M. Ooms, Christina M. Lucato, Andrew M. Ellisdon, Christina A. Mitchell; P-Rex1 and P-Rex2 RacGEFs and cancer. Biochem Soc Trans 15 August 2017; 45 (4): 963–977. doi: https://doi.org/10.1042/BST20160269
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