P-Rex1 and P-Rex2 RacGEFs and cancer. (15th August 2017)

• Record Type: Journal Article
• Authors: Srijakotre, Nuthasuda; Man, Joey; Ooms, Lisa M.; Lucato, Christina M.; Ellisdon, Andrew M.; Mitchell, Christina A.
• Is Part Of: Biochemical Society transactions. Volume 45:Number 4(2017)
• Page Start: 963
• Page End: 977
• Publication Date: 2017-08-15
• Subjects: cancer -- PREX1 -- PREX2 -- RacGEF; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST20160269
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : 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.