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Perspectives

Using kinomics to delineate signaling pathways: Control of crtc2/torc2 by the ampk family

Accalia Fu and Robert A. Screaton
Volume 7, Issue 24
December 15, 2008
Pages 3823 - 3828

This is an open-access article


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The classical role of AMP-activated protein kinase (AMPK) as an energy status sensor is expanding to include other members of the AMPK family. Recent genetic and cell biological evidence points to a role for MAP/microtubule affinity-regulating kinase 2 (MARK2/EMK/Par1b) in the regulation of metabolic events as well as in the control of CREB-dependent transcription activated by glucose in pancreatic islet beta cells. We have recently developed an in vitro kinase screening platform to identify novel kinase: Substrate pairs, the building blocks of signal transduction pathways. Application of this technology led us to identify MARK2 as the kinase that targets a novel glucose-regulated phosphorylation site on Transducer of Regulated CREB Activity 2 (TORC2, referred to as CREB-Regulated Transcriptional Coactivator 2, or CRTC2), a transcriptional coactivator essential for CREB activity in beta cells. We discuss these recent developments and suggest a model whereby members of the AMPK family integrate numerous signals to coordinate energy metabolism and cellular polarity with gene expression to regulate cell function/proliferation.


Authors

Accalia Fu
Children's Hospital of Eastern Ontario; Ottawa, ON
Robert A. Screaton
Children's Hospital of Eastern Ontario; Ottawa, ON

This is an open-access article


 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.

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