The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Functional Nanoscale Organization of Signaling Molecules Downstream of the T Cell Antigen Receptor
Open accessAbstract
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 (PALM) 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 adapter 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 adapter 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.
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Cites
Imaging Intracellular Fluorescent Proteins at Nanometer Resolution
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Self-citationCell Signaling by Receptor Tyrosine Kinases
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T cell receptor ligation induces the formation of dynamically regulated signaling assemblies
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Cited by
Phase separation of signaling molecules promotes T cell receptor signal transduction
Su, X., Ditlev, J. A., Hui, E., Xing, W., Banjade, S., Okrut, J., King, D. S., Taunton, J., Rosen, M. K., & Vale, R. D. (2016) · Science · doi:10.1126/science.aad9964 · Cited by 1,246
T cell receptor signalling networks: branched, diversified and bounded
Brownlie, R. J., & Zamoyska, R. (2013) · Nature Reviews Immunology · doi:10.1038/nri3403 · Cited by 453
Tracking single molecules at work in living cells
Kusumi, A., Tsunoyama, T. A., Hirosawa, K. M., Kasai, R. S., & Fujiwara, T. K. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1558 · Cited by 332
Nanoclustering as a dominant feature of plasma membrane organization
Garcia-Parajo, M. F., Cambi, A., Torreno-Pina, J. A., Thompson, N., & Jacobson, K. (2014) · Journal of Cell Science · doi:10.1242/jcs.146340 · Cited by 284
Glycerol Monolaurate (GML) inhibits human T cell signaling and function by disrupting lipid dynamics
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Metadata
- Authors
- Sherman, E., Barr, V., Manley, S., Patterson, G., Balagopalan, L., Akpan, I., Regan, C. K., Merrill, R. K., Sommers, C. L., Lippincott-Schwartz, J., & Samelson, L. E.
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2011-11
- Volume
- 35
- Issue
- 5
- Pages
- 705-720
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W2135630804
- Cited by
- 309
- References
- 39
- FWCI
- 10.43
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Sherman, E., Barr, V., Manley, S., Patterson, G., Balagopalan, L., Akpan, I., Regan, C. K., Merrill, R. K., Sommers, C. L., Lippincott-Schwartz, J., & Samelson, L. E. (2011). Functional Nanoscale Organization of Signaling Molecules Downstream of the T Cell Antigen Receptor. Immunity. https://doi.org/10.1016/j.immuni.2011.10.004
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