PodcastCancer

Science Signaling Podcast: 31 March 2015

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Sci. Signal.  31 Mar 2015:
Vol. 8, Issue 370, pp. pc8
DOI: 10.1126/scisignal.aab1358

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Abstract

This Podcast features an interview with Sarah Mense and Ramon Parsons, authors of a Research Article that appears in the 31 March 2015 issue of Science Signaling, about how cancer-associated mutations in PREX2 overcome the tumor-suppressive effects of the phosphatase and tensin homolog (PTEN). PTEN is a tumor suppressor that inhibits cell proliferation and cell migration, both of which contribute to cancer progression. The cell migration protein PREX2 inhibits the lipid phosphatase activity of PTEN, thereby reducing the ability of PTEN to suppress cell proliferation. Mense et al. discovered that PTEN and PREX2 reciprocally inhibit one another. PTEN suppressed cell migration and invasion by directly inhibiting PREX2 and did so independently of its lipid phosphatase activity. Cancer-associated mutant forms of PREX2 could not be inhibited by PTEN but were still able to inhibit the lipid phosphatase activity of PTEN. Thus, cancer-associated mutant forms of PREX2 can promote tumor progression in two ways—by inhibiting the ability of PTEN to suppress cell proliferation and by evading inhibition by PTEN to promote invasion. In human tumor samples, high PTEN expression correlated with the presence of PREX2 mutations, suggesting that PREX2 mutations are a mechanism for overcoming the tumor-suppressive effects of PTEN.

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