Unknown

Dataset Information

0

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


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 TCR? 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.

SUBMITTER: Sherman E 

PROVIDER: S-EPMC3225724 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications


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 activati  ...[more]

Similar Datasets

| S-EPMC7415668 | biostudies-literature
| S-EPMC4281300 | biostudies-literature
| S-EPMC6546920 | biostudies-literature
2012-08-28 | E-GEOD-40403 | biostudies-arrayexpress
| S-EPMC6944503 | biostudies-literature
| S-EPMC4689545 | biostudies-literature
2021-06-14 | PXD020481 | Pride
2012-08-28 | GSE40403 | GEO
| S-EPMC3865716 | biostudies-literature
| S-EPMC2193139 | biostudies-literature