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Science China Life Sciences

, Volume 56, Issue 7, pp 653–660

First Online: 31 May 2013Received: 21 April 2013Accepted: 09 May 2013DOI: 10.1007-s11427-013-4494-0

Cite this article as: Xin, F. & Wu, J. Sci. China Life Sci. 2013 56: 653. doi:10.1007-s11427-013-4494-0

Abstract

The mitogen-activated protein kinase MAPK p38α is a key regulator in many cellular processes, whose activity is tightly regulated by upstream kinases, phosphatases and other regulators. Transforming growth factor-β activated kinase 1 TAK1 is an upstream kinase in p38α signaling, and its full activation requires a specific activator, the TAK1-binding protein TAB1. TAB1 was also shown to be an inducer of p38α’s autophosphorylation and-or a substrate driving the feedback control of p38α signaling. Here we determined the complex structure of the unphosphorylated p38α and a docking peptide of TAB1, which shows that the TAB1 peptide binds to the classical MAPK docking groove and induces long-range conformational changes on p38α. Our structural and biochemical analyses suggest that TAB1 is a reasonable substrate of p38α, yet the interaction between the docking peptide and p38α may not be sufficient to trigger trans-autophosphorylation of p38α.

Keywordsp38α MAP kinase TAB1 KIM crystal structure This article is published with open access at Springerlink.com

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Autor: FengJiao Xin - JiaWei Wu

Fuente: https://link.springer.com/







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