How does the kinase Lck phosphorylate the T cell receptor? Spatial organization as a regulatory mechanism

Rossy, Jérémie; Williamson, David J.; Gaus, Katharina

How does the kinase Lck phosphorylate the T cell receptor? Spatial organization as a regulatory mechanism

Files

Rossy_2-z4r5kqx9fv5i6.pdf(1.89 MB)

Date

2012

Authors

Rossy, Jérémie

Williamson, David J.

Gaus, Katharina

Publication type

Journal article

Publication status

Published

Published in

Frontiers in immunology ; 3 (2012). - 167. - eISSN 1664-3224

Abstract

T cell signaling begins with the ligation of the T cell antigen receptor (TCR) by a cognate peptide and the phosphorylation of the receptor's immunoreceptor tyrosine-based activation motif domains by the kinase Lck. However, the canonical receptor model is insufficient to explain how the constitutively active kinase Lck can discriminate between non-ligated and ligated TCRs. Here, we discuss the factors that are thought to regulate the spatial distribution of the TCR and Lck, and therefore critically influence TCR signaling initiation.

Subject (DDC)

570 Biosciences, Biology

Cite This

ISO 690

ROSSY, Jérémie, David J. WILLIAMSON, Katharina GAUS, 2012. How does the kinase Lck phosphorylate the T cell receptor? Spatial organization as a regulatory mechanism. In: Frontiers in immunology. 3, 167. eISSN 1664-3224. Available under: doi: 10.3389/fimmu.2012.00167

BibTex

@article{Rossy2012kinas-43470,
  year={2012},
  doi={10.3389/fimmu.2012.00167},
  title={How does the kinase Lck phosphorylate the T cell receptor? Spatial organization as a regulatory mechanism},
  volume={3},
  journal={Frontiers in immunology},
  author={Rossy, Jérémie and Williamson, David J. and Gaus, Katharina},
  note={Article Number: 167}
}

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Refereed

Yes