Regulation of integrin function by T cell activation: Points of convergence and divergence

Traci Zell, Wendy J. Kivens, Sirid Aiměe Kellermann, Yoji Shimizu

Research output: Contribution to journalReview articlepeer-review

25 Scopus citations


Lymphocyte adhesiveness is dynamically regulated in response to conditions in the extracellular environment. One mechanism of regulation of integrin adhesion receptors involves a rapid, but transient, increase in integrin function upon T lymphocyte activation. These integrin activating signals can be initiated either via ligation of Ig superfamily members that are coupled to tyrosine kinase cascades, such as the CD3/T cell receptor, CD2, and CD28, or by G protein-coupled receptors for chemokines. Analysis of integrin activation induced by CD3/TCR, CD2 and CD28 suggests a critical role for phosphoinositide 3-OH kinase (PI 3-K). This review summarizes recent insights into PI 3-K-dependent regulation of integrin function in leukocytes, including the mechanisms by which these receptors are coupled to PI 3-K, and potential downstream effecters of PI 3-K that regulate integrin-mediated adhesion in leukocytes.

Original languageEnglish (US)
Pages (from-to)127-145
Number of pages19
JournalImmunologic Research
Issue number2
StatePublished - 1999


  • Adhesion
  • CD2
  • CD28
  • CD3
  • Integrin
  • PI 3-kinase
  • Signaling
  • T lymphocyte


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