TRIP6 transcriptional co-activator is a novel substrate of AMP-activated protein kinase

Cellular Signalling
Maria Carmen Solaz-FusterPascual Sanz

Abstract

AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that acts as a sensor of cellular energy charge. Once activated it switches on catabolic pathways and switches off many ATP-consuming processes (anabolic pathways) to preserve the energy status of the cell. In order to identify new targets of AMPK action we have performed a two-hybrid screening of a human pancreas cDNA library. As a result, we have identified TRIP6 as a novel target of AMPK action. This protein belongs to the zyxin family of proteins located at the focal adhesion plaques in the plasma membrane, although they may also travel to the nucleus, where they have regulatory properties. We confirmed the physical interaction between the catalytic subunit (AMPK-alpha2) of the AMPK complex and TRIP6 in mammalian cells by two-hybrid and co-immunoprecipitation assays. We also showed that AMPK was able to phosphorylate in vitro TRIP6 at the N-terminus. Finally, we present evidence that transcriptional co-activator properties of TRIP6 were enhanced by AMPK action.

References

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Citations

Jul 1, 2008·American Journal of Physiology. Lung Cellular and Molecular Physiology·Xia ZhaoEdward Abraham
Jul 5, 2007·Proceedings of the National Academy of Sciences of the United States of America·Sibylle JägerBruce M Spiegelman
Jul 21, 2009·The International Journal of Biochemistry & Cell Biology·Daniel MorenoPascual Sanz
Dec 1, 2015·Nature Communications·Yan YanTomi P Mäkelä
Nov 8, 2011·Biology of the Cell·Semjon WillierThomas G P Grunewald
Jul 22, 2014·Developmental Dynamics : an Official Publication of the American Association of Anatomists·Yun-Ju LaiTsu-Wei Wang
Nov 22, 2007·Human Molecular Genetics·Maria Carmen Solaz-FusterSantiago Rodriguez de Córdoba
Aug 15, 2013·The Journal of Biological Chemistry·Navin ViswakarmaJanardan K Reddy
Oct 27, 2015·BMC Biochemistry·Rosa VianaPascual Sanz
Aug 23, 2007·The Journal of Biological Chemistry·Eric L GreerAnne Brunet

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