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International Immunology Advance Access originally published online on February 16, 2007
International Immunology 2007 19(4):391-400; doi:10.1093/intimm/dxm004
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© The Japanese Society for Immunology. 2007. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

KLRG1 binds cadherins and preferentially associates with SHIP-1

Marlowe S. Tessmer1, Céline Fugere1, Frederik Stevenaert2, Olga V. Naidenko3, H. Jonathan Chong1, Georges Leclercq2 and Laurent Brossay1

1 Department of Molecular Microbiology and Immunology and Graduate Program in Pathobiology, Division of Biology and Medicine, Box G-B618, Brown University, Providence, RI 02912, USA
2 Department of Clinical Chemistry, Microbiology and Immunology, University of Ghent, Ghent, Belgium
3 Department of Pathology and Immunology, Washington University School of Medicine, St Louis, MO, USA

Correspondence to: L. Brossay; E-mail: laurent_brossay{at}brown.edu

The killer cell lectin-like receptor G1 (KLRG1) is a unique inhibitory receptor expressed on a phenotypically mature subset of resting NK cells as well as subsets of T cells in naive mice. In vivo, pathogenic immune system activation induces dramatic changes in the expression patterns of KLRG1 among the different cell subsets. In order to enhance our understanding of KLRG1 signaling properties and to clarify the functions of KLRG1 on these cells, we identified the broadly expressed N-cadherin molecule as a ligand for KLRG1. We further demonstrate that a second member of this superfamily of adhesion molecules, E-cadherin, binds to KLRG1. Additionally, we show that upon phosphorylation of the immunoreceptor tyrosine-based inhibitory motif (ITIM) tyrosine, KLRG1 recruits both SHIP-1 and SHP-2 but not SHP-1. We also delineate the key KLRG1 ITIM amino acid residues required for optimal association with these phosphatases. Finally, we demonstrate that KLRG1 engagement can inhibit sub-optimal TCR signaling. Taken together, our results indicate that KLRG1 may differentially regulate NK cell and T cell functions through the association with different ligands as well as the recruitment of distinct phosphatases.

Keywords: cell surface molecules, natural killer cells, signal transduction

Transmitting editor: E. Vivier

Received 11 December 2006, accepted 15 January 2007.


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