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Functional nanoscale organization of signaling molecules downstream of the T cell antigen receptor.

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Immunity. 2011 Nov 23;35(5):705-20. doi: 10.1016/j.immuni.2011.10.004
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Functional nanoscale organization of signaling molecules downstream of the T cell antigen receptor. Lippincott-Schwartz Lab
Sherman E, Barr V, Manley S, Patterson G, Balagopalan L, Akpan I, Regan CK, Merrill RK, Sommers CL, Lippincott-Schwartz J, Samelson LE
Note: Research in this publication was not performed at Janelia.
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Abstract

Receptor-regulated cellular signaling often is mediated by formation of transient, heterogeneous protein complexes of undefined structure. We used single and two-color photoactivated localization microscopy to study complexes downstream of the T cell antigen receptor (TCR) in single-molecule detail at the plasma membrane of intact T cells. The kinase ZAP-70 distributed completely with the TCRζ chain and both partially mixed with the adaptor LAT in activated cells, thus showing localized activation of LAT by TCR-coupled ZAP-70. In resting and activated cells, LAT primarily resided in nanoscale clusters as small as dimers whose formation depended on protein-protein and protein-lipid interactions. Surprisingly, the adaptor SLP-76 localized to the periphery of LAT clusters. This nanoscale structure depended on polymerized actin and its disruption affected TCR-dependent cell function. These results extend our understanding of the mechanism of T cell activation and the formation and organization of TCR-mediated signaling complexes, findings also relevant to other receptor systems.

PMID: 22055681 [PubMed - indexed for MEDLINE]

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Janelia Authors

Jennifer Lippincott-Schwartz
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