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The Journal of Immunology, 2002, 169: 55-62.
Copyright © 2002 by The American Association of Immunologists

2B4 Is Constitutively Associated with Linker for the Activation of T Cells in Glycolipid-Enriched Microdomains: Properties Required for 2B4 Lytic Function1

Jennifer Klem*,{dagger}, Pamela C. Verrett*, Vinay Kumar{ddagger} and John D. Schatzle2,*

* Department of Pathology and {dagger} Graduate Program in Immunology, University of Texas Southwestern Medical Center, Dallas, TX 75390; and {ddagger} Department of Pathology, University of Chicago, Chicago, IL 60637

2B4 is a receptor belonging to the Ig superfamily and is found on all murine NK cells as well as a small subset of T cells. Previous studies have found that cross-linking of the 2B4 receptor results in both increased cytotoxicity and IFN-{gamma} secretion. We have discovered that 2B4 from transfected NK and T cell lines, as well as from primary murine cells, coimmunoprecipitates with the phosphoprotein linker for the activation of T cells (LAT), which is essential for TCR-mediated signaling. This association is independent of both 2B4 phosphorylation and the cytoplasmic tail of 2B4. We have found that, along with LAT, 2B4 is constitutively located in glycolipid-enriched microdomains of the plasma membrane. In fact, 2B4 appears to associate with LAT only when it localizes to glycolipid-enriched microdomains. This localization of 2B4 occurs due to a CxC cysteine motif found in the transmembrane region, as determined by mutagenesis studies. 2B4-mediated cytotoxicity is defective in the absence of LAT, indicating that LAT is a required intermediate for 2B4 signal transduction. However, we have also shown that LAT association alone is not sufficient for maximal 2B4 activation.




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