PodcastStructural Biology

Science Signaling Podcast: 14 October 2014

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Sci. Signal.  14 Oct 2014:
Vol. 7, Issue 347, pp. pc28
DOI: 10.1126/scisignal.2005939

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Abstract

This Podcast features an interview with Kai-En Chen, Tzu-Ching Meng, and Andrew Wang, authors of a Research Article that appears in the 14 October 2014 issue of Science Signaling, about their crystal structure of the MAP kinase p38γ bound to the phosphatase that inactivates it. When activated, members of the Ras superfamily of small GTPases promote cell survival and stimulate cell proliferation, and mutations that cause overactivation of Ras can cause cells to become cancerous. Many mitogen-activated protein kinases (MAPKs) cooperate with Ras to promote oncogenesis. However, the phosphorylated, active form of the MAPK p38γ suppresses Ras-induced oncogenesis, whereas the unphosphorylated, inactive form of p38γ promotes Ras-induced oncogensis. Chen et al. solved the crystal structure of p38γ bound to the phosphatase that inactivates it, PTPN3.

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