Cited by 31

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

Yamasaki, Sho, Takamatsu, Masako, Iwashima, Makio·1996·Molecular and Cellular Biology

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1128/mcb.16.12.7151

Cites

80 of 80 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

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
Antigen receptor tail clue
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
Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor
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-citation
Profound 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
The cytoplasmic domain of the T cell receptor ζ chain is sufficient to couple to receptor-associated signal transduction pathways
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
Myristylation and palmitylation of Src family members: The fats of the matter
Resh, M. D. (1994) · Cell · doi:10.1016/0092-8674(94)90104-x · Cited by 699
Two Binding Orientations for Peptides to the Src SH3 Domain: Development of a General Model for SH3-Ligand Interactions
Feng, S., Chen, J. K., Yu, H., Simon, J. A., & Schreiber, S. L. (1994) · Science · doi:10.1126/science.7526465 · Cited by 687
SIGNAL TRANSMISSION BETWEEN THE PLASMA MEMBRANE AND NUCLEUS OF T LYMPHOCYTES
Crabtree, G. R., & Clipstone, N. A. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.005145 · Cited by 635
C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains
Clark, S. G., Stern, M., & Horvitz, H. R. (1992) · Nature · doi:10.1038/356340a0 · Cited by 593
Partial T cell signaling: Altered phospho-? and lack of zap70 recruitment in APL-induced T cell anergy
Sloan‐Lancaster, J. (1994) · Cell · doi:10.1016/0092-8674(94)90080-9 · Cited by 585
Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus
Takeya, T., & Hanafusa, H. (1983) · Cell · doi:10.1016/0092-8674(83)90073-9 · Cited by 563
pp59fyn mutant mice display differential signaling in thymocytes and peripheral T cells
Stein, P. L., Lee, H.-M., Rich, S. S., & Soriano, P. M. (1992) · Cell · doi:10.1016/0092-8674(92)90308-y · Cited by 557
Essential role for ZAP-70 in both positive and negative selection of thymocytes
Negishi, I., Motoyama, N., Nakayama, K.-I., Nakayama, K., Senju, S., Hatakeyama, S., Zhang, Q., Chan, A. C., & Loh, D. Y. (1995) · Nature · doi:10.1038/376435a0 · Cited by 554
Defective T cell receptor signaling and CD8+ thymic selection in humans lacking Zap-70 kinase
Arpaia, E., Shahar, M., Dadi, H., Cohen, A., & Rolfman, C. M. (1994) · Cell · doi:10.1016/0092-8674(94)90368-9 · Cited by 554
Human Severe Combined Immunodeficiency Due to a Defect in ZAP-70, a T Cell Tyrosine Kinase
Elder, M. E., Lin, D., Clever, J. L., Chan, A. C., Hope, T. J., Weiss, A., & Parslow, T. G. (1994) · Science · doi:10.1126/science.8202712 · Cited by 512
ζ Phosphorylation Without ZAP-70 Activation Induced by TCR Antagonists or Partial Agonists
Madrenas, J., Wange, R. L., Wang, J. L., Isakov, N., Samelson, L. E., & Germain, R. N. (1995) · Science · doi:10.1126/science.7824949 · Cited by 505
Defective T cell receptor signaling in mice lacking the thymic isoform of p59fyn
Appleby, M. W., Gross, J. A., Cooke, M. P., Levin, S. D., Qian, X., & Perlmutter, R. M. (1992) · Cell · doi:10.1016/0092-8674(92)90309-z · Cited by 499
ZAP-70 Deficiency in an Autosomal Recessive form of Severe Combined Immunodeficiency
Chan, A. C., Kadlecek, T. A., Elder, M. E., Filipovich, A. H., Kuo, W.-L., Iwashima, M., Parslow, T. G., & Weiss, A. (1994) · Science · doi:10.1126/science.8202713 · Cited by 494
Self-citation
Requirement for the coexpression of T3 and the T cell antigen receptor on a malignant human T cell line.
Weiss, A., & Stobo, J. D. (1984) · The Journal of experimental medicine · doi:10.1084/jem.160.5.1284 · Cited by 493
Co-association of CD3ζ with a receptor (CD16) for IgG Fc on human natural killer cells
Lanier, L. L., Yu, G., & Phillips, J. H. (1989) · Nature · doi:10.1038/342803a0 · Cited by 436
T cell activation by clustered tyrosine kinases
Kolanus, W., Romeo, C., & Seed, B. (1993) · Cell · doi:10.1016/0092-8674(93)90304-9 · Cited by 369
Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function.
Chan, A. C., Dalton, M., Johnson, R., Kong, G. H., Wang, T., Thoma, R., & Kurosaki, T. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07247.x · Cited by 358
Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor
Hatada, M. H., Lu, X., Laird, E. R., Green, J., Morgenstern, J. P., Lou, M., Marr, C. S., Phillips, T. B., Ram, M. K., Theriault, K., et al. (1995) · Nature · doi:10.1038/377032a0 · Cited by 351
Characterization of the nuclear and cytoplasmic components of the lymphoid-specific nuclear factor of activated T cells (NF-AT) complex.
Northrop, J. P., Ullman, K. S., & Crabtree, G. R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53861-8 · Cited by 343
Altered T cell receptor signaling and disrupted T cell development in mice lacking Itk
Liao, X. C., & Littman, D. R. (1995) · Immunity · doi:10.1016/1074-7613(95)90065-9 · Cited by 315
The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor.
Donovan, J. A., Wange, R. L., Langdon, W. Y., & Samelson, L. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31595-8 · Cited by 285
Syk Protein-tyrosine Kinase Is Regulated by Tyrosine-phosphorylated Iga/Ig/3 Immunoreceptor Tyrosine Activation Motif Binding and Autophosphorylation
Rowleyt, R. B., Burkhardtt, A. L., Chao, H.-G., Matsueda, G. R., & Bolen, J. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.19.11590 · Cited by 274
Tandem SH2 domains of ZAP-70 bind to T cell antigen receptor zeta and CD3 epsilon from activated Jurkat T cells.
Wange, R. L., Malek, S. N., Desiderio, S. V., & Samelson, L. E. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36584-6 · Cited by 272
New nomenclature for the Reth motif (or ARH1/TAM/ARAM/YXXL)
Cambier, J. C. (1995) · Immunology Today · doi:10.1016/0167-5699(95)80105-7 · Cited by 268
A kinase-independent function of Lck in potentiating antigen-specific T cell activation
Xu, H., & Littman, D. R. (1993) · Cell · doi:10.1016/0092-8674(93)90511-n · Cited by 255
ZAP-70 is constitutively associated with tyrosine-phosphorylated TCR ζ in murine thymocytes and lymph node T cells
van Oers, N. S. C., Killeen, N. P., & Welss, A. (1994) · Immunity · doi:10.1016/1074-7613(94)90038-8 · Cited by 252
Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement.
Saouaf, S. J., Mahajan, S., Rowley, R. B., Kut, S. A., Fargnoli, J., Burkhardt, A. L., Tsukada, S., Witte, O. N., & Bolen, J. B. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.20.9524 · Cited by 242
Cell growth cycle block of T cell hybridomas upon activation with antigen.
Ashwell, J. D., Cunningham, R. E., Noguchi, P., & Hernández, D. (1987) · The Journal of Experimental Medicine · doi:10.1084/jem.165.1.173 · Cited by 226
Identification by electrospray ionization mass spectrometry of the sites of tyrosine phosphorylation induced in activated Jurkat T cells on the protein tyrosine kinase ZAP-70.
Watts, J. D., Affolter, M., Krebs, D. L., et al. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43911-7 · Cited by 217
CD3-negative natural killer cells express ε TCR as part of a novel molecular complex
Anderson, P., Caligiuri, M. A., Ritz, J., & Schlossman, S. F. (1989) · Nature · doi:10.1038/341159a0 · Cited by 209
Bruton tyrosine kinase is tyrosine phosphorylated and activated in pre-B lymphocytes and receptor-ligated B cells.
Aoki, Y., Isselbacher, K. J., & Pillai, S. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10606 · Cited by 195
Syk Is Activated by Phosphotyrosine-containing Peptides Representing the Tyrosine-based Activation Motifs of the High Affinity Receptor for IgE
Shiue, L., Zoller, M. J., & Brugge, J. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.18.10498 · Cited by 195
The SH3 Domain-binding T Cell Tyrosyl Phosphoprotein p120
Fukazawa, T., Reedquist, K. A., Trüb, T., Soltoff, S. P., Panchamoorthy, G., Druker, B. J., Cantley, L. C., Shoelson, S. E., & Band, H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.19141 · Cited by 186
Activating and Inhibitory Mutations in Adjacent Tyrosines in the Kinase Domain of ZAP-70
Wange, R. L., Guitián, R., Isakov, N., Watts, J. D., Aebersold, R. H., & Samelson, L. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18730 · Cited by 183
B-cell antigen receptor stimulation activates the human Bruton's tyrosine kinase, which is deficient in X-linked agammaglobulinemia.
de Weers, M., Brouns, G. S., Hinshelwood, S., Kinnon, C., Schuurman, R. K. B., Hendriks, R. W., & Borst, J. G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51014-6 · Cited by 178
Effects of p56 lck Deficiency on the Growth and Cytolytic Effector Function of an Interleukin-2-Dependent Cytotoxic T-Cell Line
Karnitz, L. M., Sutor, S. L., Torigoe, T., Reed, J. C., Bell, M. P., McKEAN, D. J., Leibson, P. J., & Abraham, R. T. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.10.4521 · Cited by 173
Binding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a Src homology 3 domain-mediated interaction.
Cheng, G., Ye, Z. S., & Baltimore, D. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.8152 · Cited by 171
Two-step TCRζ/CD3-CD4 and CD28 signaling in T cells: SH2/SH3 domains, protein-tyrosine and lipid kinases
Rudd, C. E., Janßen, O., Cai, Y.-C., da Silva, A. J., Raab, M., & Prasad, K. V. S. (1994) · Immunology Today · doi:10.1016/0167-5699(94)90248-8 · Cited by 171
Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra‐ and intermolecular interactions.
Erpel, T., Superti‐Furga, G., & Courtneidge, S. A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07077.x · Cited by 162
p56lck interacts via its src homology 2 domain with the ZAP-70 kinase.
Duplay, P., Thome, M., Hervé, F., & Acuto, O. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.179.4.1163 · Cited by 159
Binding of ZAP-70 to Phosphorylated T-Cell Receptor ζ and η Enhances Its Autophosphorylation and Generates Specific Binding Sites for SH2 Domain-Containing Proteins
Neumeister, E. N., Zhu, Y., Richard, S., et al. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.6.3171 · Cited by 158
Identification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling.
Yamanashi, Y., Okada, M., Semba, T., Yamori, T., Umemori, H., Tsunasawa, S., Toyoshima, K., Kitamura, D., Watanabe, T., & Yamamoto, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3631 · Cited by 153
The Structural Biology of CD2
Moingeon, P. E., Chang, H., Sayre, P. H., et al. (1989) · Immunological Reviews · doi:10.1111/j.1600-065x.1989.tb00544.x · Cited by 150
Isolation and characterization of a novel human gene expressed specifically in the cells of hematopoietic lineage.
Kitamura, D., Kaneko, H., Miyagoe, Y., Ariyasu, T., & Watanabe, T. (1989) · Europe PMC (PubMed Central) · Cited by 146
Isolation and characterization of a T-lymphocyte somatic mutant with altered signal transduction by the antigen receptor.
Goldsmith, M. A., & Weiss, A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.19.6879 · Cited by 141
Phosphatidylinositol (PI) 3-Kinase and PI 4-Kinase Binding to the CD4-p56 lck Complex: the p56 lck SH3 Domain Binds to PI 3-Kinase but Not PI 4-Kinase
Prasad, K. V., Kapeller, R., Janßen, O., Repke, H., Duke‐Cohan, J. S., Cantley, L. C., & Rudd, C. E. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7708 · Cited by 140
Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation.
Abraham, N., & Veillette, A. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.10.5197 · Cited by 130
The Btk subfamily of cytoplasmic tyrosine kinases: structure, regulation and function
Rawlings, D. J. (1995) · Seminars in Immunology · doi:10.1006/smim.1995.0028 · Cited by 127
Antigen‐receptor induced clonal expansion and deletion of lymphocytes are impaired in mice lacking HS1 protein, a substrate of the antigen‐receptor‐coupled tyrosine kinases.
Taniuchi, I., Kitamura, D., Maekawa, Y., Fukuda, T., Kishi, H., & Watanabe, T. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00036.x · Cited by 123
Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen.
Sewell, W. A., Brown, M. H., Dunne, J., Owen, M. J., & Crumpton, M. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.22.8718 · Cited by 123
p56lck-independent activation and tyrosine phosphorylation of p72syk by T-cell antigen receptor/CD3 stimulation.
Couture, C., Baier, G., Altman, A., & Mustelin, T. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5301 · Cited by 112
Absence of ZAP-70 prevents signaling through the antigen receptor on peripheral blood T cells but not on thymocytes.
Gelfand, E. W., Weinberg, K. I., Mazer, B. D., et al. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.4.1057 · Cited by 104
SH2 Domain Function Is Essential for the Role of the Lck Tyrosine Kinase in T Cell Receptor Signal Transduction
Straus, D. B., Chan, A. C., Patai, B., & Weiss, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.17.9976 · Cited by 99
Syk and ZAP-70 mediate recruitment of p56lck/CD4 to the activated T cell receptor/CD3/zeta complex.
Thome, M., Duplay, P., Guttinger, M., & Acuto, O. (1995) · The Journal of experimental medicine · doi:10.1084/jem.181.6.1997 · Cited by 98
Activation of p56 lck by p72 syk through Physical Association and N-Terminal Tyrosine Phosphorylation†
Couture, C., Baier, G., Oetken, C., Williams, S., Telford, D. J., Marie‐Cardine, A., Baier, G., Fischer, S., Burn, P., Altman, A., et al. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.8.5249 · Cited by 97
Reconstitution of Syk function by the ZAP-70 protein tyrosine kinase
Kong, G.-H., Bu, J.-Y., Kurosaki, T., Shaw, A. S., & Chant, A. C. (1995) · Immunity · doi:10.1016/1074-7613(95)90029-2 · Cited by 97
Structural requirements for enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck.
Caron, L., Abraham, N., Pawson, T. J., & Veillette, A. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.6.2720 · Cited by 88
TCR Activation of ZAP70 Is Impaired in CD4+CD8+ Thymocytes as a Consequence of Intrathymic Interactions that Diminish Available p56lck
Wiest, D. L., Ashe, J. M., Abe, R., Bolen, J. B., & Singer, A. (1996) · Immunity · doi:10.1016/s1074-7613(00)80415-x · Cited by 86
LckBP1, a proline‐rich protein expressed in haematopoietic lineage cells, directly associates with the SH3 domain of protein tyrosine kinase p56lck.
Takemoto, Y., Furuta, M., Li, X., Strong-Sparks, W. J., & Hashimoto, Y. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07346.x · Cited by 79
The SH3 Domain of p56 lck Is Involved in Binding to Phosphatidylinositol 3′-Kinase from T Lymphocytes
Vogel, L. B., & Fujita, D. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7408-7417.1993 · Cited by 79
Rapid T-cell receptor-mediated tyrosine phosphorylation of p120, an Fyn/Lck Src homology 3 domain-binding protein.
Reedquist, K. A., Fukazawa, T., Druker, B. J., et al. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.10.4135 · Cited by 77
The Ras GTPase-activating Protein (GAP) Is an SH3 Domain-binding Protein and Substrate for the Src-related Tyrosine Kinase, Hck
Briggs, S. D., Bryant, S. S., Jove, R., Sanderson, S. D., & Smithgall, T. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.24.14718 · Cited by 76
In vitro characterization of major ligands for Src homology 2 domains derived from protein tyrosine kinases, from the adaptor protein SHC and from GTPase‐activating protein in Ramos B cells
Baumann, G., Maier, D., Freuler, F., Tschopp, C., Baudisch, K., & Wienands, J. (1994) · European Journal of Immunology · doi:10.1002/eji.1830240812 · Cited by 67
Ras GTPase-activating protein: a substrate and a potential binding protein of the protein-tyrosine kinase p56lck.
Amrein, K. E., Flint, N., Panholzer, B., & Burn, P. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.8.3343 · Cited by 63
Restoration of surface IgM-mediated apoptosis in an anti-IgM-resistant variant of WEHI-231 lymphoma cells by HS1, a protein-tyrosine kinase substrate.
Fukuda, T., Kitamura, D., Taniuchi, I., Maekawa, Y., Benhamou, L. E., Sarthou, P., & Watanabe, T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.16.7302 · Cited by 63
An SH3-binding Site Conserved in Bruton's Tyrosine Kinase and Related Tyrosine Kinases Mediates Specific Protein Interactions in Vitro and in Vivo
Yang, W., Malek, S. N., & Desiderio, S. V. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.35.20832 · Cited by 52
Physical and functional interactions of protein tyrosine kinases, p59fyn and ZAP-70, in T cell signaling
Fusaki, N., Matsuda, S., Nishizumi, H., Umemori, H., & Yamamoto, T. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.4.1369 · Cited by 46
The Src homology 2 domain of the protein-tyrosine kinase p56lck mediates both intermolecular and intramolecular interactions.
Amrein, K. E., Panholzer, B., Flint, N. A., Bannwarth, W., & Burn, P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.21.10285 · Cited by 36
CD2 and the regulation of T cell anergy
Bell, G. M., & Imboden, J. B. (1995) · The Journal of Immunology · doi:10.4049/jimmunol.155.6.2805 · Cited by 25
Accumulation of p60lck in HTLV‐I‐transformed T Cell Lines Detected by an Anti‐Lck Monoclonal Antibody, MOL 171
Moroi, Y., Koga, Y., Nakamura, K., Ohtsu, M., Kimura, G., & Nomoto, K. (1991) · Japanese Journal of Cancer Research · doi:10.1111/j.1349-7006.1991.tb01920.x · Cited by 20

Research works printed but not linked: 5

10.1128/mcb.10.10.5197-5206.1990 · DOI
10.1128/mcb.12.6.2720-2729.1992 · DOI
10.1128/mcb.14.8.5249-5258.1994 · DOI
10.1128/mcb.12.10.4521-4530.1992 · DOI
10.1128/mcb.13.12.7708-7717.1993 · DOI

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

See all 31

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
DOI: 10.1128/mcb.16.12.7151
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.

The Kinase, SH3, and SH2 Domains of Lck Play Critical Roles in T-Cell Activation after ZAP-70 Membrane Localization

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources