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Sci. Signal., 2 March 2010
Vol. 3, Issue 111, p. pe8
[DOI: 10.1126/scisignal.3111pe8]

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Allosteric Protein Kinase Regulation by Pseudokinases: Insights from STRAD

Thanashan Rajakulendran1,2 and Frank Sicheri1,2*

1 Centre for Systems Biology, Samuel Lunenfeld Research Institute, Toronto, Ontario M5G 1X5, Canada.
2 Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada.

Abstract: Protein kinases regulate a plethora of diverse cellular functions. Their highly controlled activation is subject to an equally diverse repertoire of regulatory mechanisms. Pseudokinases, a class of proteins that possess a structurally related protein kinase domain that lacks phospho-transfer function, are emerging as critical yet mysterious regulators of other protein kinases. A new structural and functional analysis of the pseudokinase STRAD provides insight into the mechanism by which it allosterically regulates the catalytic function of the protein kinase LKB1 and hints at an evolution from a classical kinase-substrate relationship.

* Corresponding author. E-mail, sicheri{at}lunenfeld.ca

Citation: T. Rajakulendran, F. Sicheri, Allosteric Protein Kinase Regulation by Pseudokinases: Insights from STRAD. Sci. Signal. 3, pe8 (2010).

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