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Science 14 July 1995: Vol. 269. no. 5221, pp. 242 - 244 DOI: 10.1126/science.7618087
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Articles
Science, Vol 269, Issue 5221, 242-244
Copyright © 1995 by American Association for the Advancement of Science
A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP
GM Doody,
LB Justement,
CC Delibrias,
RJ Matthews,
J Lin,
ML Thomas,
and
DT Fearon
Wellcome Trust Immunology Unit, Department of Medicine, University of Cambridge, School of Clinical Medicine, UK.
CD22 is a membrane immunoglobulin (mIg)-associated protein of B cells. CD22 is tyrosine-phosphorylated when mIg is ligated. Tyrosine-phosphorylated CD22 binds and activates SHP, a protein tyrosine phosphatase known to negatively regulate signaling through mIg. Ligation of CD22 to prevent its coaggregation with mIg lowers the threshold at which mIg activates the B cell by a factor of 100. In secondary lymphoid organs, CD22 may be sequestered away from mIg through interactions with counterreceptors on T cells. Thus, CD22 is a molecular switch for SHP that may bias mIg signaling to anatomic sites rich in T cells.
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- Expression of Dominant-Negative Src-Homology Domain 2-Containing Protein Tyrosine Phosphatase-1 Results in Increased Syk Tyrosine Kinase Activity and B Cell Activation.
- L. B. Dustin, D. R. Plas, J. Wong, Y. T. Hu, C. Soto, A. C. Chan, and M. L. Thomas (1999)
J. Immunol.
162, 2717-2724
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- Specificity of the SH2 Domains of SHP-1 in the Interaction with the Immunoreceptor Tyrosine-Based Inhibitory Motif-Bearing Receptor gp49B.
- L. L. Wang, J. Blasioli, D. R. Plas, M. L. Thomas, and W. M. Yokoyama (1999)
J. Immunol.
162, 1318-1323
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- Definition of the Sites of Interaction between the Protein Tyrosine Phosphatase SHP-1 and CD22.
- J. Blasioli, S. Paust, and M. L. Thomas (1999)
J. Biol. Chem.
274, 2303-2307
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- Inhibitory Receptors and Their Modes of Action.
- D.C. FONG and J.C. CAMBIER (1999)
Cold Spring Harb Symp Quant Biol
64, 329-334
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- The Carboxyl-terminal Region of Biliary Glycoprotein Controls Its Tyrosine Phosphorylation and Association with Protein-tyrosine Phosphatases SHP-1 and SHP-2 in Epithelial Cells.
- M. Huber, L. Izzi, P. Grondin, C. Houde, T. Kunath, A. Veillette, and N. Beauchemin (1999)
J. Biol. Chem.
274, 335-344
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- Internalization of the Lymphocytic Surface Protein CD22 Is Controlled by a Novel Membrane Proximal Cytoplasmic Motif.
- C. H. T. Chan, J. Wang, R. R. French, and M. J. Glennie (1998)
J. Biol. Chem.
273, 27809-27815
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- Recruitment and Activation of SHP-1 Protein-tyrosine Phosphatase by Human Platelet Endothelial Cell Adhesion Molecule-1 (PECAM-1). IDENTIFICATION OF IMMUNORECEPTOR TYROSINE-BASED INHIBITORY MOTIF-LIKE BINDING MOTIFS AND SUBSTRATES.
- C. T. Hua, J. R. Gamble, M. A. Vadas, and D. E. Jackson (1998)
J. Biol. Chem.
273, 28332-28340
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- SLP-76 Is a Direct Substrate of SHP-1 Recruited to Killer Cell Inhibitory Receptors.
- B. A. Binstadt, D. D. Billadeau, B. L. Williams, N. Fang, T. Yi, G. A. Koretzky, R. T. Abraham, and P. J. Leibson (1998)
J. Biol. Chem.
273, 27518-27523
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- Cutting Edge: The B Cell Surface Protein CD72 Recruits the Tyrosine Phosphatase SHP-1 upon Tyrosine Phosphorylation.
- T. Adachi, H. Flaswinkel, H. Yakura, M. Reth, and T. Tsubata (1998)
J. Immunol.
160, 4662-4665
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- SHP-1 Phosphatase C-Terminus Interacts With Novel Substrates p32/p30 During Erythropoietin and Interleukin-3 Mitogenic Responses.
- W. Yang, M. Tabrizi, K. Berrada, and T. Yi (1998)
Blood
91, 3746-3755
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- A Double-Edged Kinase Lyn: A Positive and Negative Regulator for Antigen Receptor-mediated Signals.
- H. Nishizumi, K. Horikawa, I. Mlinaric-Rascan, and T. Yamamoto (1998)
J. Exp. Med.
187, 1343-1348
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- Roles of the Complex Formation of SHPS-1 with SHP-2 in Insulin-stimulated Mitogen-activated Protein Kinase Activation.
- T. Takada, T. Matozaki, H. Takeda, K. Fukunaga, T. Noguchi, Y. Fujioka, I. Okazaki, M. Tsuda, T. Yamao, F. Ochi, et al. (1998)
J. Biol. Chem.
273, 9234-9242
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- SHP-1 Binds and Negatively Modulates the c-Kit Receptor by Interaction with Tyrosine 569 in the c-Kit Juxtamembrane Domain.
- M. Kozlowski, L. Larose, F. Lee, D. M. Le, R. Rottapel, and K. A. Siminovitch (1998)
Mol. Cell. Biol.
18, 2089-2099
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- Spontaneous Follicular Exclusion of SHP1-deficient B Cells Is Conditional on the Presence of Competitor Wild-type B Cells.
- K. N. Schmidt, C. W. Hsu, C. T. Griffin, C. C. Goodnow, and J. G. Cyster (1998)
J. Exp. Med.
187, 929-937
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- Inhibition of the B Cell by CD22: A Requirement for Lyn.
- K. G.C. Smith, D. M. Tarlinton, G. M. Doody, M. L. Hibbs, and D. T. Fearon (1998)
J. Exp. Med.
187, 807-811
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- Cutting Edge: Lyn-Mediated Down-Regulation of B Cell Antigen Receptor Signaling: Inhibition of Protein Kinase C Activation by Lyn in a Kinase-Independent Fashion.
- H. Katsuta, S. Tsuji, Y. Niho, T. Kurosaki, and D. Kitamura (1998)
J. Immunol.
160, 1547-1551
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- Association of Tyrosine Phosphatases SHP-1 and SHP-2, Inositol 5-Phosphatase SHIP with gp49B1, and Chromosomal Assignment of the Gene.
- A. Kuroiwa, Y. Yamashita, M. Inui, T. Yuasa, M. Ono, A. Nagabukuro, Y. Matsuda, and T. Takai (1998)
J. Biol. Chem.
273, 1070-1074
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- The Protein-tyrosine Phosphatase SHP-2 Associates with Tyrosine-phosphorylated Adhesion Molecule PECAM-1 (CD31).
- K. Sagawa, T. Kimura, M. Swieter, and R. P. Siraganian (1997)
J. Biol. Chem.
272, 31086-31091
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- What Goes Up Must Come Down: The Emerging Spectrum of Inhibitory Receptors.
- W. M. Yokoyama (1997)
J. Exp. Med.
186, 1803-1808
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- Btk dosage determines sensitivity to B cell antigen receptor cross-linking.
- A. B. Satterthwaite, H. Cheroutre, W. N. Khan, P. Sideras, and O. N. Witte (1997)
PNAS
94, 13152-13157
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- CD19 and CD22 expression reciprocally regulates tyrosine phosphorylation of Vav protein during B lymphocyte signaling.
- S. Sato, P. J. Jansen, and T. F. Tedder (1997)
PNAS
94, 13158-13162
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- Downregulated Expression of SHP-1 in Burkitt Lymphomas and Germinal Center B Lymphocytes.
- C. C. Delibrias, J. E. Floettmann, M. Rowe, and D. T. Fearon (1997)
J. Exp. Med.
186, 1575-1583
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