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Science 14 July 1995:
Vol. 269. no. 5221, pp. 242 - 244
DOI: 10.1126/science.7618087

Articles

Science, Vol 269, Issue 5221, 242-244
Copyright © 1995 by American Association for the Advancement of Science


articles

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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C. H. T. Chan, J. Wang, R. R. French, and M. J. Glennie (1998)
J. Biol. Chem. 273, 27809-27815
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »



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