The DOI matches its Crossref record; 80 of the 80 references it cites were found in a registry or an index.
The Kinase, SH3, and SH2 Domains of Lck Play Critical Roles in T-Cell Activation after ZAP-70 Membrane Localization
Abstract
Antigenic stimulation of the T-cell antigen receptor initiates signal transduction through the immunoreceptor tyrosine-based activation motifs (ITAMs). When its two tyrosines are phosphorylated, ITAM forms a binding site for ZAP-70, one of the cytoplasmic protein tyrosine kinases essential for T-cell activation. The signaling process that follows ZAP-70 binding to ITAM has been analyzed by the construction of fusion proteins that localize ZAP-70 to the plasma membrane. We found that membrane-localized forms of ZAP-70 induce late signaling events such as activation of nuclear factor of activated T cells without any stimulation. This activity was observed only when Lck was expressed and functional. In addition, each mutation that affects the function of Lck in the kinase, Src homology 2 (SH2), and SH3 domains greatly impaired the signaling ability of the chimeric protein. Therefore, Lck functions in multiple manners in T-cell activation for the steps following ZAP-70 binding to ITAM.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Transient or stable membrane association of ZAP-70 mediated by the membrane-permeable synthetic ligand FK1012A or by a myristoylation sequence -tagged ZAP70 (Myr-ZAP-70) can activate downstream signaling of TCR[35], [36].”
From RhoH Regulates Subcellular Localization of ZAP-70 and Lck in T Cell Receptor Signaling (2010) · cites this paper as [36]
In the citing paper
“Membrane-bound ZAP-70 can activate TCR minimally without stimuli, but still requires functional Lck activity [35], [36].”
From RhoH Regulates Subcellular Localization of ZAP-70 and Lck in T Cell Receptor Signaling (2010) · cites this paper as [36]
Citations
Cites
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
Protein modules and signalling networks
Pawson, T. (1995) · Nature · doi:10.1038/373573a0 · Cited by 2,420
Signal transduction by lymphocyte antigen receptors
Weiss, A., & Littman, D. R. (1994) · Cell · doi:10.1016/0092-8674(94)90334-4 · Cited by 2,089
RETH, M. (1989) · Nature · doi:10.1038/338383b0 · Cited by 1,438
Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A
Flanagan, W. M., Corthésy, B., Bram, R. J., & Crabtree, G. R. (1991) · Nature · doi:10.1038/352803a0 · Cited by 1,057
Straus, D. B. (1992) · Cell · doi:10.1016/0092-8674(92)90428-f · Cited by 1,044
ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR ζ chain
Chan, A. C., Iwashima, M., Turck, C. W., & Weiss, A. (1992) · Cell · doi:10.1016/0092-8674(92)90598-7 · Cited by 1,041
Self-citationProfound block in thymocyte development in mice lacking p56lck
Molina, T. J., Kishihara, K., Siderovski, D. P., van Ewijk, W., Narendran, A., Timms, E. M., Wakeham, A. C., Paige, C. J., Hartmann, K.-U., Veillette, A., et al. (1992) · Nature · doi:10.1038/357161a0 · Cited by 970
Irving, B. A., & Weiss, A. (1991) · Cell · doi:10.1016/0092-8674(91)90314-o · Cited by 819
Sequential Interactions of the TCR with Two Distinct Cytoplasmic Tyrosine Kinases
Iwashima, M., Irving, B. A., van Oers, N. S. C., Chan, A. C., & Weiss, A. (1994) · Science · doi:10.1126/science.7509083 · Cited by 716
Self-citation
Cited by
Molecular mechanisms in B cell antigen receptor signaling
Kurosaki, T. (1997) · Current Opinion in Immunology · doi:10.1016/s0952-7915(97)80075-1 · Cited by 150
RhoH Regulates Subcellular Localization of ZAP-70 and Lck in T Cell Receptor Signaling
Chae, H.-D., Siefring, J. E., Hildeman, D. A., Gu, Y., & Williams, D. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013970 · Cited by 35
Metadata
- Authors
- Yamasaki, S., Takamatsu, M., & Iwashima, M.
- Affiliations
- Division of Cell and Information, Precursory Research for Embryonic Science and Technology, Research Development Corporation of Japan
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1996-12
- Volume
- 16
- Issue
- 12
- Pages
- 7151-7160
- ISSN
- 1098-5549
- Cited by
- 31
- References
- 80
- Language
- en
- Licence
- journals.asm.org/non-commercial-tdm-license (tdm)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
