Response Multilayered Control of T Cell Receptor Phosphorylation

We would like to respond to the Correspondence by Fernandes et al., but first we will summarize the data in our Cell paper (Xu et al., 2008). Our study used a biophysical approach to examine the binding of the CD3ɛ cytoplasmic domain (CD3ɛCD) to the plasma membrane. We reported a new FRET assay to examine CD3ɛCD binding to the inner leaflet of the plasma membrane in live Jurkat cells, a transformed T cell line. Furthermore, we developed an approach to determine the NMR structure of CD3ɛCD bound in a lipid bilayer environment.

[1]  Rajat Varma,et al.  T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster. , 2006, Immunity.

[2]  D. Aivazian,et al.  Phosphorylation of T cell receptor ζ is regulated by a lipid dependent folding transition , 2000, Nature Structural Biology.

[3]  M. Gresser,et al.  Mechanism of Inhibition of Protein-tyrosine Phosphatases by Vanadate and Pervanadate* , 1997, The Journal of Biological Chemistry.

[4]  T. Meyer,et al.  PI(3,4,5)P3 and PI(4,5)P2 Lipids Target Proteins with Polybasic Clusters to the Plasma Membrane , 2006, Science.

[5]  S. McLaughlin,et al.  Binding of Peptides with Basic and Aromatic Residues to Bilayer Membranes , 2003, Journal of Biological Chemistry.

[6]  G. G. Stokes.  "J." , 1890, The New Yale Book of Quotations.

[7]  L. Wilkinson.  Immunity , 1891, The Lancet.

[8]  Tony Yeung,et al.  Membrane Phosphatidylserine Regulates Surface Charge and Protein Localization , 2008, Science.

[9]  Simon J Davis,et al.  The kinetic-segregation model: TCR triggering and beyond , 2006, Nature Immunology.

[10]  Amy M Becker,et al.  The Cytoplasmic Tail of the T Cell Receptor CD3 ε Subunit Contains a Phospholipid-Binding Motif that Regulates T Cell Functions1 , 2009, The Journal of Immunology.

[11]  Etienne Gagnon,et al.  Regulation of T Cell Receptor Activation by Dynamic Membrane Binding of the CD3ɛ Cytoplasmic Tyrosine-Based Motif , 2008, Cell.

[12]  J. Partanen,et al.  The human p50csk tyrosine kinase phosphorylates p56lck at Tyr‐505 and down regulates its catalytic activity. , 1992, The EMBO journal.