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Structural analysis of the PTEN:P-Rex2 signaling complex reveals how cancer-associated mutations coordinate to hyperactivate Rac1.

Science signaling - 4 May 2021

D'Andrea Laura, Lucato Christina M, Marquez Elsa A, Chang Yong-Gang, Civciristov Srgjan, Mastos Chantel, Lupton Christopher J, Huang Cheng, Elmlund Hans, Schittenhelm Ralf B, Mitchell Christina A, Whisstock James C, Halls Michelle L, Ellisdon Andrew M

Abstract excerpt

The dual-specificity phosphatase PTEN functions as a tumor suppressor by hydrolyzing PI(3,4,5)P3 to PI(4,5)P2 to inhibit PI3K-AKT signaling and cellular proliferation. P-Rex2 is a guanine nucleotide exchange factor for Rho GTPases and can be activated by Gβγ subunits downstream of G protein-coupled receptor signaling and by PI(3,4,5)P3 downstream of receptor tyrosine kinases. The PTEN:P-Rex2 complex is a commonly...

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PMID: 33947796
DOI: 10.1126/scisignal.abc4078

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