title: alpha beta T cell receptor ligand-specific oligomerization revisited.
abstract: The mechanism of T cell receptor signaling is unclear. Included among models for TCR signaling is ligand-induced oligomerization in a fashion analogous to other cell surface receptors. Published kinetic, saturation binding, and light scattering experiments have been interpreted to suggest a propensity for soluble alpha beta TCR/peptide/MHC ectodomain complexes to oligomerize. Upon performing these experiments with soluble ectodomains of human class I and class II restricted alpha beta TCRs, we find no evidence for dimerization or oligomerization of complexes. Apparently, oligomerization in solution to a detectable extent is not a general property of soluble alpha beta TCRs or their complexes with ligand. Our results suggest that membrane-anchored, fully assembled TCRs should be studied to determine the role oligomerization plays in T cell signaling.
authors: Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA.
authors: B M
authors: BM
authors: Baker
authors: D C
authors: DC
authors: Wiley
mesh_terms: D000818:Animals; D015789:HLA-A2 Antigen / Q000276:immunology; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008285:Major Histocompatibility Complex; D051379:Mice; D018448:Models, Immunological; D009842:Oligopeptides / Q000276:immunology; D010455:Peptides / Q000276:immunology; D016693:Receptors, Antigen, T-Cell, alpha-beta / Q000276:immunology*; D020349:Surface Plasmon Resonance; D013696:Temperature; D014461:Ultracentrifugation
chemical_list: D015789:HLA-A2 Antigen; D008024:Ligands; D009842:Oligopeptides; D010455:Peptides; D016693:Receptors, Antigen, T-Cell, alpha-beta