Src Homology Region 2 Domain-Containing Phosphatase 1 Positively Regulates B Cell Receptor-Induced Apoptosis by Modulating Association of B Cell Linker Protein with Nck and Activation of c-Jun NH2-Terminal Kinase

Mizuno, Kazuya; Tagawa, Yuko; Mitomo, Katsuyuki; Watanabe, Noriyuki; Katagiri, Tatsuo; Ogimoto, Mami; Yakura, Hidetaka

doi:10.4049/jimmunol.169.2.778

Cited by 34Protein Tyrosine PhosphatasesT-cell and B-cell ImmunologyProtein Kinase Regulation and GTPase Signaling

Src Homology Region 2 Domain-Containing Phosphatase 1 Positively Regulates B Cell Receptor-Induced Apoptosis by Modulating Association of B Cell Linker Protein with Nck and Activation of c-Jun NH2-Terminal Kinase

Open access

Mizuno, Kazuya, Tagawa, Yuko, Mitomo, Katsuyuki, Watanabe, Noriyuki, Katagiri, Tatsuo, Ogimoto, Mami, Yakura, Hidetaka·2002·The Journal of Immunology

DOI 10.4049/jimmunol.169.2.778

Open this paper in CoChat — free account Open PDF

Abstract

Src homology region 2 domain-containing phosphatase 1 (SHP-1) is a key mediator in lymphocyte differentiation, proliferation, and activation. We previously showed that B cell linker protein (BLNK) is a physiological substrate of SHP-1 and that B cell receptor (BCR)-induced activation of c-Jun NH2-terminal kinase (JNK) is significantly enhanced in cells expressing a form of SHP-1 lacking phosphatase activity (SHP-1-C/S). In this study, we confirmed that SHP-1 also exerts negative regulatory effects on JNK activation in splenic B cells. To further clarify the role of SHP-1 in B cells, we examined how dephosphorylation of BLNK by SHP-1 affects downstream signaling events. When a BLNK mutant (BLNKΔN) lacking the NH2-terminal region, which contains four tyrosine residues, was introduced in SHP-1-C/S-expressing WEHI-231 cells, the enhanced JNK activation was inhibited. Among candidate proteins likely to regulate JNK activation through BLNK, Nck adaptor protein was found to associate with tyrosine-phosphorylated BLNK and this association was more pronounced in SHP-1-C/S-expressing cells. Furthermore, expression of dominant-negative forms of Nck inhibited BCR-induced JNK activation. Finally, BCR-induced apoptosis was suppressed in SHP-1-C/S-expressing cells and coexpression of Nck SH2 mutants or a dominant-negative form of SEK1 reversed this phenotype. Collectively, these results suggest that SHP-1 acts on BLNK, modulating its association with Nck, which in turn negatively regulates JNK activation but exerts a positive effect on apoptosis.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.4049/jimmunol.169.2.778

Cites

54 of 54 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Alternative signaling pathways through CD38, CD40, IL-4R, LPS/TLR4/MyD88, and CD86 also utilize PLCγ2, while TGF-βR stimulation inhibits PLCγ2 function in B cells.
“Aside from BCR engagement, there are alternative signaling pathways initiated through extracellular immunological receptors that also utilize PLCγ2 to function, which include CD38 (16), CD40 (52), IL-4R (53, 54, 55) and the LPS/TLR4/MyD88 pathway, the latter of which induces ERK and NK-κB phosphorylation in MEKs in a PI3K-independent fashion (56). CD86 engagement was also observed to signal via PL”
From The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration (2021) · cites this paper as [53]
The introductory passage (section C; page unavailable) mentions phospholipase Cγ as a protein recruited by BLNK after BCR ligation, not through the alternative receptors in the claim. Searches for CD38, CD40, IL-4R, LPS/TLR4/MyD88, CD86, and TGF-βR found no passage establishing their claimed effects on PLCγ2. (LLM, conf=0.76)
Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Signal transduction by the JNK group of MAP kinases
Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237 · see citing works
The small GTP-binding proteins Rac1 and Cdc42regulate the activity of the JNK/SAPK signaling pathway
Coso, O. A., Chiariello, M., Yu, J., Teramoto, H., Crespo, P., Xu, N., Miki, T., & Gutkind, J. S. (1995) · Cell · doi:10.1016/s0092-8674(05)80018-2 · Cited by 1,629 · see citing works
Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers
Schaeffer, H. J., & Weber, M. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2435 · Cited by 1,600 · see citing works
Signal transduction by the c-Jun N-terminal kinase (JNK) — from inflammation to development
Ip, Y. T., & Davis, R. J. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80143-9 · Cited by 1,538 · see citing works
Selective activation of the JNK signaling cascadeand c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
Minden, A., Lin, A., Claret, F.-X., Abo, A., & Karin, M. (1995) · Cell · doi:10.1016/s0092-8674(05)80019-4 · Cited by 1,481 · see citing works
The Jnk1 and Jnk2 Protein Kinases Are Required for Regional Specific Apoptosis during Early Brain Development
Kuan, C.-Y., Yang, D. D., Roy, D. R. S., Davis, R. J., RAKIC, P. T., & Flavell, R. A. (1999) · Neuron · doi:10.1016/s0896-6273(00)80727-8 · Cited by 889 · see citing works
Early Lethality, Functional NF-κB Activation, and Increased Sensitivity to TNF-Induced Cell Death in TRAF2-Deficient Mice
Yeh, W., Shahinian, A., Speiser, D. E., Kraunus, J., Billia, F., Wakeham, A. C., de la Pompa, J. L., Ferrick, D. A., Hum, B., Iscove, N. N., et al. (1997) · Immunity · doi:10.1016/s1074-7613(00)80391-x · Cited by 798 · see citing works
Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene
Shultz, L. D., Schweitzer, P. A., Rajan, T. V., Yi, T., Ihle, J. N., Matthews, R. J., Thomas, M. L., & Beier, D. R. (1993) · Cell · doi:10.1016/0092-8674(93)90369-2 · Cited by 741 · see citing works
Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1
Yan, M., Dai, T., Deak, J. C., Kyriakis, J. M., Zon, L. I., Woodgett, J. R., & Templeton, D. J. (1994) · Nature · doi:10.1038/372798a0 · Cited by 705 · see citing works
Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene
Tsui, H. W., Siminovitch, K. A., de Souza, L., & Tsui, F. W. L. (1993) · Nature Genetics · doi:10.1038/ng0693-124 · Cited by 564 · see citing works
MODULAR PEPTIDE RECOGNITION DOMAINS IN EUKARYOTIC SIGNALING
Kuriyan, J., & Cowburn, D. (1997) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.26.1.259 · Cited by 549 · see citing works
A Role in B Cell Activation for CD22 and the Protein Tyrosine Phosphatase SHP
Doody, G. M., Justement, L. B., Delibrias, C., Matthews, R. J., Lin, J., Thomas, M. L., & Fearon, D. T. (1995) · Science · doi:10.1126/science.7618087 · Cited by 538 · see citing works
Untitled work
Fu (1998) · doi:10.1016/s1074-7613(00)80591-9 · Cited by 518 · see citing works
INITIATION AND PROCESSING OF SIGNALS FROM THE B CELL ANTIGEN RECEPTOR
Reth, M. G., & Wienands, J. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.453 · Cited by 436 · see citing works
GENETIC ANALYSIS OF B CELL ANTIGEN RECEPTOR SIGNALING
Kurosaki, T. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.555 · Cited by 433 · see citing works
Signal Transduction by the B Cell Antigen Receptor and its Coreceptors
Cambier, J. C., Pleiman, C. M., & Clark, M. R. (1994) · Annual Review of Immunology · doi:10.1146/annurev.iy.12.040194.002325 · Cited by 411 · see citing works
Protein tyrosine phosphatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection
Cyster, J. G., & Goodnow, C. C. (1995) · Immunity · doi:10.1016/1074-7613(95)90075-6 · Cited by 394 · see citing works
Defective neural tube morphogenesis and altered apoptosis in the absence of both JNK1 and JNK2
Sabapathy, K., Jochum, W., Hochedlinger, K., Chang, L., Karin, M., & Wagner, E. F. (1999) · Mechanisms of Development · doi:10.1016/s0925-4773(99)00213-0 · Cited by 359 · see citing works
Matrix Survival Signaling
Almeida, E. A. C., Ilić, D., Han, Q., Hauck, C. R., Jin, F., Kawakatsu, H., Schlaepfer, D. D., & Damsky, C. H. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.3.741 · Cited by 355 · see citing works
The complexity of signaling pathways activated by the BCR
DeFranco, A. L. (1997) · Current Opinion in Immunology · doi:10.1016/s0952-7915(97)80074-x · Cited by 318 · see citing works
BLNK Required for Coupling Syk to PLCγ2 and Rac1-JNK in B Cells
Ishiai, M., Kurosaki, M., Pappu, R., Okawa, K., Ronko, I., Fu, C., Shibata, M., Iwamatsu, A., Chan, A. C., & Kurosaki, T. (1999) · Immunity · doi:10.1016/s1074-7613(00)80012-6 · Cited by 318 · see citing works
Requirement for B Cell Linker Protein (BLNK) in B Cell Development
Pappu, R., Cheng, A. M., Li, B., Gong, Q., Chiu, C. W., Griffin, N., White, J. M., Sleckman, B. P., & Chan, A. C. (1999) · Science · doi:10.1126/science.286.5446.1949 · Cited by 305 · see citing works
SLP-65: A New Signaling Component in B Lymphocytes which Requires Expression of the Antigen Receptor for Phosphorylation
Wienands, J., Schweikert, J., Wollscheid, B., Jumaa, H., Nielsen, P. J., & Reth, M. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.4.791 · Cited by 271 · see citing works
Human HPK1, a novel human hematopoietic progenitor kinase that activates the JNK/SAPK kinase cascade.Preprint
Hu, M. C. ‐., Qiu, W., Wang, X., Meyer, C. F., & Tan, T. (1996) · Genes & Development · doi:10.1101/gad.10.18.2251 · Cited by 255 · see citing works
NIK is a new Ste20‐related kinase that binds NCK and MEKK1 and activates the SAPK/JNK cascade via a conserved regulatory domain
Su, Y. C., Han, J., Xu, S., Cobb, M. H., & Skolnik, E. Y. (1997) · The EMBO Journal · doi:10.1093/emboj/16.6.1279 · Cited by 255 · see citing works
Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the regulation of B cell signaling.
Pani, G., Kozlowski, M., Cambier, J. C., Mills, G. B., & Siminovitch, K. A. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.181.6.2077 · Cited by 251 · see citing works
HPK1, a hematopoietic protein kinase activating the SAPK/JNK pathway.
Kiefer, F., Tibbles, L. A., Anafi, M., Janssen, A., Zanke, B. W., Lassam, N. J., Pawson, T. J., Woodgett, J. R., & Iscove, N. N. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01093.x · Cited by 242 · see citing works
Differential activation of the ERK, JNK, and p38 mitogen-activated protein kinases by CD40 and the B cell antigen receptor
Sutherland, C., Heath, A. W., Pelech, S., Young, P. R., & Gold, M. R. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.157.8.3381 · Cited by 234 · see citing works
Anti‐immunoglobulins induce death by apoptosis in WEHI‐231 B lymphoma cells
Benhamou, L. E., Cazenave, P., & Sarthou, P. (1990) · European Journal of Immunology · doi:10.1002/eji.1830200630 · Cited by 234 · see citing works
Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3
Lehmann, J. M., Riethmüller, G., & Johnson, J. P. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.4.1048 · Cited by 210 · see citing works
Requirement of SH2-containing Protein Tyrosine Phosphatases SHP-1 and SHP-2 for Paired Immunoglobulin-like Receptor B (PIR-B)–mediated Inhibitory Signal
Maeda, A., Kurosaki, M., Ono, M., Takai, T., & Kurosaki, T. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.8.1355 · Cited by 203 · see citing works
Intramolecular Regulation of Protein Tyrosine Phosphatase SH-PTP1: A New Function for Src Homology 2 Domains
Pei, D., Lorenz, U. M., Klingmüller, U., Neel, B. G., & Walsh, C. T. (1994) · Biochemistry · doi:10.1021/bi00255a030 · Cited by 198 · see citing works
Involvement of stress-activated protein kinase and p38 mitogen-activated protein kinase in mIgM-induced apoptosis of human B lymphocytes
Graves, J. D., Draves, K. E., Craxton, A., Saklatvala, J., Krebs, E. G., & Clark, E. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13814 · Cited by 161 · see citing works
The B cell surface protein CD72 recruits the tyrosine phosphatase SHP-1 upon tyrosine phosphorylation.
Adachi, T., Flaswinkel, H., Yakura, H., Reth, M. G., & Tsubata, T. (1998) · PubMed · Cited by 156 · see citing works
Self-citation
Cutting Edge: The B Cell Surface Protein CD72 Recruits the Tyrosine Phosphatase SHP-1 upon Tyrosine Phosphorylation
Adachi, T., Flaswinkel, H., Yakura, H., Reth, M. G., & Tsubata, T. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.10.4662 · Cited by 146 · see citing works
Self-citation
BASH, a novel signaling molecule preferentially expressed in B cells of the bursa of Fabricius.
Goitsuka, R., Fujimura, Y., Mamada, H., Umeda, A., Morimura, T., Uetsuka, K., Doi, K., Tsuji, S., & Kitamura, D. (1998) · PubMed · Cited by 145 · see citing works
The B-cell transmembrane protein CD72 binds to and is an in vivo substrate of the protein tyrosine phosphatase SHP-1.
Wu, Y.-J., Nadler, M. J. S., Brennan, L., Gish, G., Timms, J., Fusaki, N., Jongstra-Bilen, J., Tada, N., Pawson, T., Wither, J., et al. (1998) · Current Biology · doi:10.1016/s0960-9822(07)00421-6 · Cited by 143 · see citing works
HPK1 Is Activated by Lymphocyte Antigen Receptors and Negatively Regulates AP-1
Liou, J., Kiefer, F., Dang, A., Hashimoto, A., Cobb, M. H., Kurosaki, T., & Weiss, A. (2000) · Immunity · doi:10.1016/s1074-7613(00)80192-2 · Cited by 140 · see citing works
The B cell-restricted adaptor BASH is required for normal development and antigen receptor-mediated activation of B cells
Hayashi, K., Nittono, R., Okamoto, N., Tsuji, S., Hara, Y., Goitsuka, R., & Kitamura, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.040575697 · Cited by 138 · see citing works
Nck-Interacting Ste20 Kinase Couples Eph Receptors to c-Jun N-Terminal Kinase and Integrin Activation
Becker, E., Huynh‐Do, U., Holland, S. J., Pawson, T. J., Daniel, T. O., & Skolnik, E. Y. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1537-1545.2000 · Cited by 131 · see citing works
Hematopoietic Progenitor Kinase 1 Associates Physically and Functionally with the Adaptor Proteins B Cell Linker Protein and SLP-76 in Lymphocytes
Sauer, K., Liou, J., Singh, S. B., Yablonski, D., Weiss, A., & Perlmutter, R. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106811200 · Cited by 129 · see citing works
Cutting Edge: BASH, A Novel Signaling Molecule Preferentially Expressed in B Cells of the Bursa of Fabricius
Goitsuka, R., Fujimura, Y., Mamada, H., Umeda, A., Morimura, T., Uetsuka, K., Doi, K., Tsuji, S., & Kitamura, D. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.11.5804 · Cited by 115 · see citing works
The Adaptor Protein BLNK Is Required for B Cell Antigen Receptor-induced Activation of Nuclear Factor-κB and Cell Cycle Entry and Survival of B Lymphocytes
Tan, J. E.-L., Wong, S. C., Gan, S. K., Xu, S., & Lam, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010800200 · Cited by 102 · see citing works
SHP-1 Requires Inhibitory Co-receptors to Down-modulate B Cell Antigen Receptor-mediated Phosphorylation of Cellular Substrates
Adachi, T., Wienands, J., Wakabayashi, C., Yakura, H., Reth, M. G., & Tsubata, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100997200 · Cited by 81 · see citing works
Self-citation
Src Homology Region 2 (SH2) Domain-Containing Phosphatase-1 Dephosphorylates B Cell Linker Protein/SH2 Domain Leukocyte Protein of 65 kDa and Selectively Regulates c-Jun NH2-Terminal Kinase Activation in B Cells
Mizuno, K., Tagawa, Y., Mitomo, K., Arimura, Y., Hatano, N., Katagiri, T., Ogimoto, M., & Yakura, H. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.3.1344 · Cited by 76 · see citing works
Self-citation
Regulation of B cell signal transduction by SH2-containing protein–tyrosine phosphatases
Siminovitch, K. A., & Neel, B. G. (1998) · Seminars in Immunology · doi:10.1006/smim.1998.0125 · Cited by 71 · see citing works
B Cell Adaptor Containing Src Homology 2 Domain (Bash) Links B Cell Receptor Signaling to the Activation of Hematopoietic Progenitor Kinase 1
Tsuji, S., Okamoto, M., Yamada, K., Okamoto, N., Goitsuka, R., Arnold, R., Kiefer, F., & Kitamura, D. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.194.4.529 · Cited by 68 · see citing works
Hematopoietic Cell Phosphatase Is Recruited to CD22 following B Cell Antigen Receptor Ligation
Lankester, A. C., van Schijndel, G. M. W., & van Lier, R. A. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.35.20305 · Cited by 68 · see citing works
Extracellular Signal-Regulated Kinase-2, But Not c-Jun NH2-Terminal Kinase, Activation Correlates with Surface IgM-Mediated Apoptosis in the WEHI 231 B Cell Line
Lee, J. R., & Koretzky, G. A. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.4.1637 · Cited by 56 · see citing works
The SH2 Domain Containing Tyrosine Phosphatase-1 Down-regulates Activation of Lyn and Lyn-induced Tyrosine Phosphorylation of the CD19 Receptor in B Cells
Somani, A.-K. B., Yuen, K., Xu, F., Zhang, J., Branch, D. R., & Siminovitch, K. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006820200 · Cited by 49 · see citing works
Negative regulation of apoptotic death in immature B cells by CD45
Ogimoto, M., Katagirl, T., Mashima, K., Hasegawa, K., Mizuno, K., & Yakura, H. (1994) · International Immunology · doi:10.1093/intimm/6.4.647 · Cited by 45 · see citing works
Self-citation
The Role of Protein Tyrosine Phosphatases in Lymphocyte Activation and Differentiation
Yakura, H. (1994) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.v14.i3-4.50 · Cited by 34 · see citing works
Self-citation
Opposing regulation of B cell receptor‐induced activation of mitogen‐activated protein kinases by CD45
Ogimoto, M., Arimura, Y., Katagiri, T., Mitomo, K., Woodgett, J. R., Nebreda, Á. R., Mizuno, K., & Yakura, H. (2001) · FEBS Letters · doi:10.1016/s0014-5793(00)02416-9 · Cited by 11 · see citing works
Self-citation
Untitled work
(1999) · doi:10.1002/(sici)1521-4141(199903)29:03
Self-citation

Flagged first, then by citations

Sorted by citations

Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization
Verma, R. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27414 · Cited by 351 · see citing works
The Murine Nck SH2/SH3 Adaptors Are Important for the Development of Mesoderm-Derived Embryonic Structures and for Regulating the Cellular Actin Network
Bladt, F., Aippersbach, E., Gelkop, S., Strasser, G. A., Nash, P., Tafuri, A., Gertler, F. B., & Pawson, T. J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.13.4586-4597.2003 · Cited by 183 · see citing works
The Role of C-terminal Tyrosine Phosphorylation in the Regulation of SHP-1 Explored via Expressed Protein Ligation
Zhang, Z., Shen, K., Lü, W., & Cole, P. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210028200 · Cited by 150 · see citing works
The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration
Jackson, J. T., Mulazzani, E., Nutt, S. L., & Masters, S. L. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100905 · Cited by 113 · see citing works
Nck adapter proteins: functional versatility in T cells
Lettau, M., Pieper, J., & Janßen, O. (2009) · Cell Communication and Signaling · doi:10.1186/1478-811x-7-1 · Cited by 105 · see citing works
Signal Transduction in Natural Killer Cells
Macfarlane, A. W., & Campbell, K. S. (2005) · Current topics in microbiology and immunology · doi:10.1007/3-540-27743-9_2 · Cited by 105 · see citing works
Evaluation of CD33 as a genetic risk factor for Alzheimer’s disease
Estus, S., Shaw, B. C., Devanney, N. A., Katsumata, Y., Press, E., & Fardo, D. W. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02000-4 · Cited by 95 · see citing works
Carcinoembryonic Antigen-Related Cellular Adhesion Molecule 1 Isoforms Alternatively Inhibit and Costimulate Human T Cell Function
Chen, D., Iijima, H., Nagaishi, T., Nakajima, A., Russell, S. E., Raychowdhury, R., Morales, V., Rudd, C. E., Utku, N., & Blumberg, R. S. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.6.3535 · Cited by 89 · see citing works
Cell penetrating peptide conjugated bioreducible polymer for siRNA delivery
Nam, H. Y., Kim, J., Kim, S., Yockman, J. W., Kim, S. W., & Bull, D. A. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.03.058 · Cited by 80 · see citing works
Vascular Endothelial Growth Factor Receptor 2 Direct Interaction with Nephrin Links VEGF-A Signals to Actin in Kidney Podocytes
Bertuccio, C. A., Verón, D., Aggarwal, P. K., Holzman, L. B., & Tufró, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.241620 · Cited by 70 · see citing works
Pivotal Advance: CEACAM1 is a negative coreceptor for the B cell receptor and promotes CD19-mediated adhesion of B cells in a PI3K-dependent manner
Lobo, E. O., Zhang, Z., & Shively, J. E. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0109037 · Cited by 49 · see citing works
Gene-expression profiling during curcumin-induced apoptosis reveals downregulation of CXCR4
Skommer, J., Włodkowic, D., & Pelkonen, J. (2006) · Experimental Hematology · doi:10.1016/j.exphem.2006.09.006 · Cited by 49 · see citing works
Antigen-Specific B-Lymphocyte Activation
Bishop, G. A., Haxhinasto, S. A., Stunz, L. L., & Hostager, B. S. (2003) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.v23.i3.10 · Cited by 46 · see citing works
RNA interference targeting SHP‐1 attenuates myocardial infarction in rats
Sugano, M., Tsuchida, K., Hata, T., & Makino, N. (2005) · The FASEB Journal · doi:10.1096/fj.05-4020fje · Cited by 40 · see citing works
B cell defects in SLP65/BLNK‐deficient mice can be partially corrected by the absence of CD22, an inhibitory coreceptor for BCR signaling
Gerlach, J., Ghosh, S., Jumaa, H., Reth, M., Wienands, J., Chan, A., & Nitschke, L. (2003) · European Journal of Immunology · doi:10.1002/eji.200324290 · Cited by 43 · see citing works
CCR3 Expression Induced by IL-2 and IL-4 Functioning as a Death Receptor for B Cells
Jinquan, T., Jacobi, H. H., Chen, J., Millner, A. H., Sten, E., Hviid, L., Anting, L., Ryder, L. P., Glue, C., Skov, P. S., et al. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.4.1722 · Cited by 33 · see citing works
Adaptor proteins in lymphocyte activation
Janssen, E., & Zhang, W. (2003) · Current Opinion in Immunology · doi:10.1016/s0952-7915(03)00044-x · Cited by 30 · see citing works
SHP-1 Inhibition by 4-Hydroxynonenal Activates Jun N-Terminal Kinase and Glutamate Cysteine Ligase
Rinna, A., & Forman, H. J. (2008) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2007-0371oc · Cited by 27 · see citing works
Simultaneous regulation of apoptotic gene silencing and angiogenic gene expression for myocardial infarction therapy: Single-carrier delivery of SHP-1 siRNA and VEGF-expressing pDNA
Kim, D., Ku, S. H., Kim, H., Jeong, J. H., Lee, M., Kwon, I. C., Choi, D., & Kim, S. H. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.10.017 · Cited by 25 · see citing works
Sub-proteomic study on macrophage response to Candida albicans unravels new proteins involved in the host defense against the fungus
Reales‐Calderón, J. A., Martínez‐Solano, L., Martínez-Gomáriz, M., Nombela, C., Molero, G., & Gil, C. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.01.037 · Cited by 23 · see citing works
SLP‐76 is recruited to CD22 and dephosphorylated by SHP‐1, thereby regulating B cell receptor‐induced c‐Jun N‐terminal kinase activation
Mizuno, K., Tagawa, Y., Watanabe, N., Ogimoto, M., & Yakura, H. (2005) · European Journal of Immunology · doi:10.1002/eji.200425465 · Cited by 27 · see citing works
Self-citation
Regulating Vav1 phosphorylation by the SHP-1 tyrosine phosphatase is a fine-tuning mechanism for the negative regulation of DISC formation and Fas-mediated cell death signaling
Koncz, G., Kerekes, K., Chakrabandhu, K., & Hueber, A. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402282 · Cited by 20 · see citing works
Dual regulation of BCR‐mediated growth inhibition signaling by CD72
Baba, T., Fusaki, N., Aoyama, A., Li, D. H., Okamura, R. M., Parnes, J. R., & Hozumi, N. (2005) · European Journal of Immunology · doi:10.1002/eji.200425775 · Cited by 18 · see citing works
Sinner or Saint?: Nck Adaptor Proteins in Vascular Biology
Alfaidi, M., Scott, M. L., & Orr, A. W. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.688388 · Cited by 16 · see citing works
Delivery of small interfering RNA for inhibition of endothelial cell apoptosis by hypoxia and serum deprivation
Cho, S., Hartle, L., Son, S. M., Yang, F., Goldberg, M. S., Xu, Q., Langer, R., & Anderson, D. G. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.08.123 · Cited by 16 · see citing works
The role of protein tyrosine phosphatases in the regulation of allergic asthma: implication of TC‐PTP and PTP‐1B in the modulation of disease development
Pouliot, P., Bergeron, S., Marette, A., & Olivier, M. (2009) · Immunology · doi:10.1111/j.1365-2567.2009.03139.x · Cited by 14 · see citing works
Myosin is an in vivo substrate of the protein tyrosine phosphatase (SHP-1) after mIgM cross-linking.
Baba, T., Fusaki, N., Shinya, N., Iwamatsu, A., & Hozumi, N. (2003) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/s0006-291x(03)00542-4 · Cited by 19 · see citing works
Comparison of polymerase chain reaction-based genotyping of Helicobacter pylori by direct polymerase chain reaction from biopsies and cultures from patients with dyspepsia in Nigeria
Smith, S. I., Jolaiya, T., Fowora, M. A., Ugiagbe, R., Onyekwere, C. A., Agbo, I. I., Lesi, O. A., Palamides, P., Adedeji, A., Ndububa, D. A., et al. (2019) · Minerva Biotecnologica · doi:10.23736/s1120-4826.19.02558-8 · Cited by 7 · see citing works
Friend or foe? Unraveling the complex roles of protein tyrosine phosphatases in cardiac disease and development
Krenz, M. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110297 · Cited by 5 · see citing works
Vanadate-Induced Inhibition of BCR-Triggered Apoptosis is Coupled with Tyrosine Phosphorylation and Induction of G2M Growth Arrest in Ramos-BL B Cells
Hristov, K. K., Knox, K. A., & Mitev, V. (2007) · Immunological Investigations · doi:10.1080/08820130601069814 · Cited by 2 · see citing works
Molecular immunogenetics of apoptosis: experimental dilemas.
Singh, R., & Reddy, L. (2012) · DUT Open Scholar (Durban University of Technology) · Cited by 1 · see citing works
Identification of therapeutic targets in the Burkitt’s lymphoma specific B cell antigen receptor signaling network
Kruse, V. (2018) · doi:10.53846/goediss-7116 · Cited by 1 · see citing works
Functioning as a Death Receptor for B Cells CCR3 Expression Induced by IL-2 and IL-4
Malling, H., Poulsen, L. K., Skov, P. S., Jarman, E., Lamberth, K., Sten, E., Hviid, L., Anting, L., Ryder, L. P., Jinquan, C. T., et al. (2013)
Recherche de facteurs génétiques impliqués dans la résistance au paludisme et au sepsis : études pangénomiques de liaison génétique et d'association, intégration des résultats d' association aux réseaux d' intéractions protéine-protéine
Brisebarre, A. (2014) · doi:10.70675/2f9e9809z53acz4bdfza1e9z874d97974954

Src Homology Region 2 (SH2) Domain-Containing Phosphatase-1 Dephosphorylates B Cell Linker Protein/SH2 Domain Leukocyte Protein of 65 kDa and Selectively Regulates c-Jun NH2-Terminal Kinase Activation in B Cells
Mizuno, K., Tagawa, Y., Mitomo, K., Arimura, Y., Hatano, N., Katagiri, T., Ogimoto, M., & Yakura, H. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.3.1344 · Cited by 76 · see citing works
Self-citation
SLP‐76 is recruited to CD22 and dephosphorylated by SHP‐1, thereby regulating B cell receptor‐induced c‐Jun N‐terminal kinase activation
Mizuno, K., Tagawa, Y., Watanabe, N., Ogimoto, M., & Yakura, H. (2005) · European Journal of Immunology · doi:10.1002/eji.200425465 · Cited by 27 · see citing works
Self-citation
Hematopoietic Progenitor Kinase 1 Associates Physically and Functionally with the Adaptor Proteins B Cell Linker Protein and SLP-76 in Lymphocytes
Sauer, K., Liou, J., Singh, S. B., Yablonski, D., Weiss, A., & Perlmutter, R. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106811200 · Cited by 129 · see citing works
Expression of Dominant-Negative Src-Homology Domain 2-Containing Protein Tyrosine Phosphatase-1 Results in Increased Syk Tyrosine Kinase Activity and B Cell Activation
Dustin, L. B., Plas, D. R., Wong, J., Hu, Y. T., Soto, C. E., Chan, A. C., & Thomas, M. L. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.5.2717 · Cited by 116 · see citing works
Down-regulation of B Cell Receptor Signaling by Hematopoietic Progenitor Kinase 1 (HPK1)-mediated Phosphorylation and Ubiquitination of Activated B Cell Linker Protein (BLNK)
Wang, X., Li, J.-P., Kuo, H.-K., Chiu, L.-L., Dement, G. A., Lan, J., Chen, D.-Y., Yang, C.-Y., Hu, H., & Tan, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.310946 · Cited by 70 · see citing works

Authors: Mizuno, K., Tagawa, Y., Mitomo, K., Watanabe, N., Katagiri, T., Ogimoto, M., & Yakura, H.
Affiliations: Tokyo Metropolitan Institute of Medical Science (JP)
ORCID: Watanabe, Noriyuki
Venue: The Journal of Immunology
Publisher: Oxford University Press (OUP)
Published: 2002-07
Volume: 169
Issue: 2
Pages: 778-786
ISSN: 0022-1767 (ISSN-L)
1550-6606
DOI: 10.4049/jimmunol.169.2.778
OpenAlex: W2099206489
Cited by: 34
References: 54
Citations by year: 2022: 1 · 2021: 2 · 2019: 2 · 2018: 1 · 2016: 1 · 2014: 1 · 2013: 1 · 2012: 2
FWCI: 1.39
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: The Journal of Immunology (publishedVersion)
PubMed (publishedVersion)
Funders: Ministry of Education, Culture, Sports, Science and Technology
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: SHP-1, Nck, c-Jun NH2-terminal kinase, JNK activation, B cell receptor signaling, apoptosis, tyrosine phosphorylation, SEK1, B cell signaling
MeSH terms: Adjuvants, Immunologic, Animals, B-Lymphocytes, Carrier Proteins, Enzyme Activation, Mice, Inbred C3H, Mice, Mutant Strains, Peptide Fragments, Phosphoproteins, Receptors, Antigen, B-Cell, Spleen, Tumor Cells, Cultured, Oncogene Proteins, Down-Regulation, Up-Regulation, Protein Tyrosine Phosphatases, Apoptosis, src Homology Domains, Mitogen-Activated Protein Kinases, Intracellular Signaling Peptides and Proteins, JNK Mitogen-Activated Protein Kinases, Adaptor Proteins, Signal Transducing, Mice, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Phosphatase 1

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

Src Homology Region 2 Domain-Containing Phosphatase 1 Positively Regulates B Cell Receptor-Induced Apoptosis by Modulating Association of B Cell Linker Protein with Nck and Activation of c-Jun NH2-Terminal Kinase

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks