Regulation of lymphocyte function by protein phosphorylation

Roger M. Perlmutter*, Steven D. Levin, Mark W. Appleby, Steven J. Anderson, Jose Alberola-Ila

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

188 Scopus citations

Abstract

Variations in protein phosphorylation provide the predominant means of enzymatic regulation now known in biological systems, especially in the regulation of signal transduction from cell surface receptors. Analysis of these signaling pathways has proceeded especially rapidly in lymphocytes, in part because these cells can be isolated with relative ease and can in many cases be maintained in vitro for prolonged periods as clonal populations. During the past few years, both biochemical and genetic evidence has been adduced indicating that the antigen receptors of T and B lymphocytes associate functionally with nonreceptor protein tyrosine kinases. Similar data implicate protein tyrosine kinases in signaling from the CD4 and CD8 coreceptors and the β chain of the IL-2 receptor. Protein serine/threonine kinases and several different phosphatases also participate in the intracellular propagation of antigen receptor-derived signals. Here we review the lymphocyte surface receptors that are believed to act by altering protein phosphorylation, the kinases and phosphatases that are believed to regulate signal transduction in lymphocytes, and the implications of these results for the broader study of cell signaling mechanisms.

Original languageEnglish (US)
Pages (from-to)451-499
Number of pages49
JournalAnnual Review of Immunology
Volume11
DOIs
StatePublished - 1993

Keywords

  • phosphotyrosine phosphatases
  • protein tyrosine kinases

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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