Cutting edge: Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells

J Immunol. 2002 Sep 15;169(6):2813-7. doi: 10.4049/jimmunol.169.6.2813.

Abstract

In resting T cells, Csk is constitutively localized in lipid rafts by virtue of interaction with a phosphorylated adaptor protein, Csk-binding protein (Cbp)/phosphoprotein associated with glycolipid-enriched microdomains, and sets an activation threshold in TCR signaling. In this study, we examined a kinase responsible for Cbp phosphorylation in T cell membrane rafts. By analyzing T cells from Fyn-/- mice, we clearly demonstrated that Fyn, but not Lck, has its kinase activity in membrane rafts, and plays a critical role in Cbp phosphorylation, Cbp-Csk interaction, and Csk kinase activity. Naive CD44(low)CD62 ligand(high) T cells were substantially reduced in Fyn-/- mice, presumably due to the inhibition of Cbp phosphorylation. Thus, Fyn mediates Cbp-Csk interaction and recruits Csk to rafts by phosphorylating Cbp. Csk recruited to rafts would then be activated and inhibit the kinase activity of Lck to keep resting T cells in a quiescent state. Our results elucidate a negative regulatory role for Fyn in proximal TCR signaling in lipid rafts.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Glycolipids / metabolism
  • Humans
  • Immunophenotyping
  • Intercellular Signaling Peptides and Proteins
  • Interphase / genetics
  • Interphase / immunology*
  • Jurkat Cells
  • Lymphocyte Count
  • Lymphocyte Specific Protein Tyrosine Kinase p56(lck) / metabolism
  • Membrane Microdomains / enzymology
  • Membrane Microdomains / metabolism*
  • Membrane Proteins / metabolism*
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein-Tyrosine Kinases / metabolism
  • Protein-Tyrosine Kinases / physiology*
  • Proto-Oncogene Proteins / deficiency
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins / physiology*
  • Proto-Oncogene Proteins c-fyn
  • Proto-Oncogene Proteins pp60(c-src)*
  • T-Lymphocyte Subsets / cytology
  • T-Lymphocyte Subsets / enzymology
  • T-Lymphocyte Subsets / metabolism*
  • Tyrosine / antagonists & inhibitors
  • Tyrosine / metabolism*

Substances

  • Adaptor Proteins, Signal Transducing
  • Glycolipids
  • Intercellular Signaling Peptides and Proteins
  • Membrane Proteins
  • PAG1 protein, human
  • Pag protein, mouse
  • Pag1 protein, mouse
  • Phosphoproteins
  • Proto-Oncogene Proteins
  • Tyrosine
  • Matk protein, mouse
  • Protein-Tyrosine Kinases
  • FYN protein, human
  • Fyn protein, mouse
  • Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
  • Proto-Oncogene Proteins c-fyn
  • Proto-Oncogene Proteins pp60(c-src)