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J Immunol. 2011 Jan 15;186(2):784-90. doi: 10.4049/jimmunol.1001562. Epub 2010 Dec 13.

Beta-catenin inhibits T cell activation by selective interference with linker for activation of T cells-phospholipase C-γ1 phosphorylation.

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1
Department of Pathology, University of Chicago, Chicago, IL 60637, USA.

Abstract

Despite the defined function of the β-catenin pathway in thymocytes, its functional role in peripheral T cells is poorly understood. We report that in a mouse model, β-catenin protein is constitutively degraded in peripheral T cells. Introduction of stabilized β-catenin into primary T cells inhibited proliferation and cytokine secretion after TCR stimulation and blunted effector cell differentiation. Functional and biochemical studies revealed that β-catenin selectively inhibited linker for activation of T cells phosphorylation on tyrosine 136, which was associated with defective phospholipase C-γ1 phosphorylation and calcium signaling but normal ERK activation. Our findings indicate that β-catenin negatively regulates T cell activation by a previously undescribed mechanism and suggest that conditions under which β-catenin might be inducibly stabilized in vivo would be inhibitory for T cell-based immunity.

PMID:
21149602
PMCID:
PMC4888792
DOI:
10.4049/jimmunol.1001562
[Indexed for MEDLINE]
Free PMC Article

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