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Related Experiment Video

Updated: Jul 13, 2026

Adenoviral Transduction of Naive CD4 T Cells to Study Treg Differentiation
15:33

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Published on: August 13, 2013

Signaling through CD43 regulates CD4 T-cell trafficking.

Purvi D Mody1, Judy L Cannon, Hozefa S Bandukwala

  • 1Committee on Immunology, University of Chicago, IL 60637, USA.

Blood
|July 20, 2007
PubMed
Summary

Phosphorylation of Ser76 in CD43 (sialophorin) is crucial for T-cell migration to lymph nodes. This finding reveals a new signaling role for CD43 in regulating T-cell trafficking and function.

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Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries
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Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries
08:49

Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries

Published on: January 22, 2019

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • CD43 (sialophorin) is a mucin-like protein involved in T-cell activation, proliferation, and migration.
  • The precise mechanism by which CD43 regulates T-cell trafficking remains incompletely understood.
  • The role of CD43 phosphorylation in its diverse cellular functions is largely unexplored.

Purpose of the Study:

  • To investigate the role of CD43 phosphorylation in regulating T-cell function, particularly T-cell trafficking.
  • To identify specific phosphorylation sites on CD43 and their functional consequences.

Main Methods:

  • Tandem mass spectrometry was employed to identify phosphorylation sites on murine CD43.
  • Site-directed mutagenesis was used to alter identified phosphorylation sites (Ser76 to alanine).
  • T-cell trafficking to lymph nodes, CD43 exclusion from the immune synapse, and T-cell proliferation were assessed.

Main Results:

  • Serine 76 (Ser76) in the cytoplasmic domain of murine CD43 was identified as a novel site of basal phosphorylation.
  • Mutation of Ser76 to alanine significantly impaired T-cell trafficking to the lymph node.
  • CD43 exclusion from the immune synapse and regulation of T-cell proliferation were unaffected by the Ser76 mutation.
  • The extracellular domain of CD43 was also found to be essential for T-cell trafficking, suggesting a role in signal transduction.

Conclusions:

  • CD43 phosphorylation at Ser76 is a critical regulator of T-cell migration.
  • CD43 acts as a signaling molecule, sensing extracellular cues and transmitting signals to modulate T-cell function.
  • These findings elucidate a novel mechanism for CD43-mediated regulation of T-cell trafficking, highlighting the importance of both its cytoplasmic and extracellular domains.