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Sci. Signal., 19 February 2013
Vol. 6, Issue 263, p. ra13
[DOI: 10.1126/scisignal.2003607]


Editor's Summary

Conformational Kinase Activation
Lck is a tyrosine kinase that is critical for T cell activation, and its activity is induced by the T cell receptor (TCR). Phosphorylation of Lck at various residues either promotes or inhibits its activity, and Lck exists in various phosphorylated states in a T cell. With fluorescence lifetime imaging microscopic analysis of live human T cells and biochemical analyses, Stirnweiss et al. found that TCR activation produced a conformational change in Lck. In vitro studies showed that this "open" conformation of Lck exhibited enhanced kinase activity. Thus, phosphorylation, location, and conformation all potentially contribute to the regulation of Lck activity.

Citation: A. Stirnweiss, R. Hartig, S. Gieseler, J. A. Lindquist, P. Reichardt, L. Philipsen, L. Simeoni, M. Poltorak, C. Merten, W. Zuschratter, Y. Prokazov, W. Paster, H. Stockinger, T. Harder, M. Gunzer, B. Schraven, T Cell Activation Results in Conformational Changes in the Src Family Kinase Lck to Induce Its Activation. Sci. Signal. 6, ra13 (2013).

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Focal Adhesion Kinase Negatively Regulates Lck Function Downstream of the T Cell Antigen Receptor.
N. M. Chapman, S. F. Connolly, E. L. Reinl, and J. C. D. Houtman (2013)
J. Immunol. 191, 6208-6221
   Abstract »    Full Text »    PDF »
Coreceptor affinity for MHC defines peptide specificity requirements for TCR interaction with coagonist peptide-MHC.
J. A. H. Hoerter, J. Brzostek, M. N. Artyomov, S. M. Abel, J. Casas, V. Rybakin, J. Ampudia, C. Lotz, J. M. Connolly, A. K. Chakraborty, et al. (2013)
J. Exp. Med. 210, 1807-1821
   Abstract »    Full Text »    PDF »

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