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Weak SLP-76-PLC-γ1 interaction in the LAT-nucleated multi-protein complex fine-tunes TCR signal strength to optimize

Hidehiro Yamane1, Junya Wada1, Elizabeth N Stassenko1

  • 1Laboratory of Cellular and Molecular Biology, Center for Cancer Research (CCR), National Cancer Institute (NCI), National Institutes of Health (NIH), Bethesda, MD, U.S.A.

Biorxiv : the Preprint Server for Biology
|September 26, 2025
PubMed

Insights

The weak interaction between SLP-76 and PLC-γ1 is crucial for T cell activation. Enhancing this interaction boosts T cell signaling, impacting immune responses and T cell development.

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Signaling

Background:

  • T cell activation involves protein tyrosine kinase recruitment and phosphorylation of adapter proteins.
  • The LAT adapter protein binds PLC-γ1 and a Gads/SLP-76 dimer, forming a heterotetramer.
  • A weak interaction exists between SLP-76 and PLC-γ1 within this complex, conserved across vertebrates.

Purpose of the Study:

  • To investigate the biological significance of the weak SLP-76-PLC-γ1 interaction.
  • To determine the role of this interaction in regulating T cell receptor (TCR) signaling strength.

Main Methods:

  • Site-directed mutagenesis was used to create an SLP-76 mutant with enhanced affinity for PLC-γ1.
  • Assessed the impact of this mutation on PLC-γ1 activity.
  • Analyzed thymocyte development and peripheral T cell responses.

Main Results:

  • The SLP-76 mutation significantly increased PLC-γ1 activity.
  • Enhanced TCR signal strength was observed.
  • Alterations in thymocyte development and peripheral T cell responses were noted.

Conclusions:

  • The conserved weak SLP-76-PLC-γ1 interaction is essential for controlled PLC-γ1 activation.
  • This interaction fine-tunes TCR signal strength, optimizing T cell-mediated immunity.

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