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As T cells and natural killer (NK) cells survey the surface of other cells, cognate receptors and ligands are commonly organized into distinct micrometer-scale domains at the intercellular contact, creating an immune or immunological synapse (IS). We aim to address the still unanswered questions of how this organization of proteins aids immune surveillance and how these domains are biophysically constructed. Molecular mechanisms for the formation of the IS include a role for the cytoskeleton, segregation of proteins according to the size of their extracellular domains, and association of proteins with lipid rafts. Towards understanding the function of the IS, it is instructive to compare and contrast the supramolecular organization of proteins at the inhibitory and activating NK cell IS with that at the activating T cell IS. Finally, it is essential to develop new technologies for probing molecular recognition at cell surfaces. Imaging parameters other than fluorescence intensity, such as the lifetime of the fluorophore's excited state, could be used to report on protein environments.

Original publication

DOI

10.1034/j.1600-065x.2002.18915.x

Type

Journal article

Journal

Immunological reviews

Publication Date

11/2002

Volume

189

Pages

179 - 192

Addresses

Department of Biological Sciences, Sir Alexander Fleming Building, Imperial College of Science, Technology and Medicine, London, UK.

Keywords

Killer Cells, Natural, T-Lymphocytes, Intercellular Junctions, Membrane Microdomains, Cytoskeleton, Animals, Humans, Mice, Membrane Proteins, Receptors, Immunologic, Ligands, Fluorescence Polarization, Fluorescence Resonance Energy Transfer, Models, Immunological