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Focal adhesion kinase negatively regulates Lck function downstream of the T cell antigen receptor
Journal article   Peer reviewed

Focal adhesion kinase negatively regulates Lck function downstream of the T cell antigen receptor

Nicole M Chapman, Sean F Connolly, Erin L Reinl and Jon C.D Houtman
The Journal of immunology (1950), Vol.191(12), pp.6208-6221
12/15/2013
DOI: 10.4049/jimmunol.1301587
PMCID: PMC3865716
PMID: 24227778

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Abstract

Focal adhesion kinase (FAK) is a critical regulator of signal transduction in multiple cell types. Although this protein is activated upon T cell receptor (TCR) engagement, the cellular function that FAK plays in mature human T cells is unknown. By suppressing the function of FAK, we revealed that FAK inhibits TCR-mediated signaling by recruiting C-terminal Src kinase (Csk) to the membrane and/or receptor complex following TCR activation. Thus, in the absence of FAK, the inhibitory phosphorylation of Lck and/or Fyn is impaired. Together, these data highlight a novel role for FAK as a negative regulator TCR function in human T cells. These results also suggest that changes in FAK expression could modulate sensitivity to TCR stimulation and contribute to the progression of T cell malignancies and autoimmune diseases.

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