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CD28 ligation induces rapid tyrosine phosphorylation of the linker molecule LAT in the absence of Syk and ZAP-70 tyrosine phosphorylation.

Publication ,  Journal Article
Tsuchida, M; Manthei, ER; Knechtle, SJ; Hamawy, MM
Published in: Eur J Immunol
July 1999

CD28 is a T cell surface molecule that is important for T cell activation. CD28-triggered T cell stimulation involves protein tyrosine phosphorylation, a process that is critical for CD28 function. Recently, a linker molecule has been identified as LAT (Linker for Activation of T cells). Studies involving LAT mutants and reconstitution experiments strongly implicate LAT in playing a critical role in T cell activation. We show in the present report that CD28 ligation induces tyrosine phosphorylation of LAT. CD28-induced tyrosine phosphorylation of LAT was rapid, as it was apparent within 1 min of CD28 ligation, reached a peak by 5 min, and declined thereafter. Previous studies implicated the protein tyrosine kinases ZAP-70 and Syk in the TCR-induced tyrosine phosphorylation of LAT. Here, tyrosine phosphorylation of Syk and ZAP-70 was detected after TCR but not after CD28 ligation. Thus, CD28 ligation appears to induce tyrosine phosphorylation of LAT by mechanisms that are independent of ZAP-70 and Syk. The concurrent ligation of CD28 and TCR increased tyrosine phosphorylation of LAT. These results implicate LAT in CD28 signal transduction pathways and in the co-stimulatory process in T cells.

Duke Scholars

Published In

Eur J Immunol

DOI

ISSN

0014-2980

Publication Date

July 1999

Volume

29

Issue

7

Start / End Page

2354 / 2359

Location

Germany

Related Subject Headings

  • ZAP-70 Protein-Tyrosine Kinase
  • Tyrosine
  • T-Lymphocytes
  • Syk Kinase
  • Signal Transduction
  • Receptors, Antigen, T-Cell
  • Protein-Tyrosine Kinases
  • Phosphorylation
  • Phosphoproteins
  • Membrane Proteins
 

Citation

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Tsuchida, M., Manthei, E. R., Knechtle, S. J., & Hamawy, M. M. (1999). CD28 ligation induces rapid tyrosine phosphorylation of the linker molecule LAT in the absence of Syk and ZAP-70 tyrosine phosphorylation. Eur J Immunol, 29(7), 2354–2359. https://doi.org/10.1002/(SICI)1521-4141(199907)29:07<2354::AID-IMMU2354>3.0.CO;2-P
Tsuchida, M., E. R. Manthei, S. J. Knechtle, and M. M. Hamawy. “CD28 ligation induces rapid tyrosine phosphorylation of the linker molecule LAT in the absence of Syk and ZAP-70 tyrosine phosphorylation.Eur J Immunol 29, no. 7 (July 1999): 2354–59. https://doi.org/10.1002/(SICI)1521-4141(199907)29:07<2354::AID-IMMU2354>3.0.CO;2-P.
Tsuchida, M., et al. “CD28 ligation induces rapid tyrosine phosphorylation of the linker molecule LAT in the absence of Syk and ZAP-70 tyrosine phosphorylation.Eur J Immunol, vol. 29, no. 7, July 1999, pp. 2354–59. Pubmed, doi:10.1002/(SICI)1521-4141(199907)29:07<2354::AID-IMMU2354>3.0.CO;2-P.
Journal cover image

Published In

Eur J Immunol

DOI

ISSN

0014-2980

Publication Date

July 1999

Volume

29

Issue

7

Start / End Page

2354 / 2359

Location

Germany

Related Subject Headings

  • ZAP-70 Protein-Tyrosine Kinase
  • Tyrosine
  • T-Lymphocytes
  • Syk Kinase
  • Signal Transduction
  • Receptors, Antigen, T-Cell
  • Protein-Tyrosine Kinases
  • Phosphorylation
  • Phosphoproteins
  • Membrane Proteins