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The Journal of Immunology, Vol 157, Issue 9 3769-3773, Copyright © 1996 by American Association of Immunologists
CUTTING EDGE |
N Fang, DG Motto, SE Ross and GA Koretzky
Graduate Program in Immunology, University of Iowa College of Medicine, Iowa City, IA 52242, USA.
SLP-76 (SH2 domain leukocyte protein of 76 kDa) is a recently identified substrate of the TCR-stimulated protein tyrosine kinases that functions in the signal transduction cascade linking the TCR with IL-2 gene expression. In this report, we demonstrate that engagement of the TCR results in tyrosine phosphorylation of SLP-76 in its amino- terminal acidic region. Two tyrosines (Y113 and Y128) fall within an identical five amino-acid motif and are shown to be phosphorylated upon TCR ligation. Although mutation of either Y113 and Y128 has a minimal effect on SLP-76 function, mutation of both residues decreases significantly the ability of SLP-76 to promote T cell activation. A third tyrosine within the amino-terminal region (Y145) appears to be the most important for optimal SLP-76 function, as altering it alone to phenylalanine has a potent impact on SLP-76 augmentation of NFAT promoter activity.
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J. Wienands, J. Schweikert, B. Wollscheid, H. Jumaa, P. J. Nielsen, and M. Reth SLP-65: A New Signaling Component in B Lymphocytes which Requires Expression of the Antigen Receptor for Phosphorylation J. Exp. Med., August 17, 1998; 188(4): 791 - 795. [Abstract] [Full Text] [PDF]
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T. Jascur, J. Gilman, and T. Mustelin Involvement of Phosphatidylinositol 3-Kinase in NFAT Activation in T Cells J. Biol. Chem., May 30, 1997; 272(22): 14483 - 14488. [Abstract] [Full Text] [PDF]
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M. A. Musci, L. R. Hendricks-Taylor, D. G. Motto, M. Paskind, J. Kamens, C. W. Turck, and G. A. Koretzky Molecular Cloning of SLAP-130, an SLP-76-associated Substrate of the T Cell Antigen Receptor-stimulated Protein Tyrosine Kinases J. Biol. Chem., May 2, 1997; 272(18): 11674 - 11677. [Abstract] [Full Text] [PDF]
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L. R. Hendricks-Taylor, D. G. Motto, J. Zhang, R. P. Siraganian, and G. A. Koretzky SLP-76 Is a Substrate of the High Affinity IgE Receptor-stimulated Protein Tyrosine Kinases in Rat Basophilic Leukemia Cells J. Biol. Chem., January 10, 1997; 272(2): 1363 - 1367. [Abstract] [Full Text] [PDF]
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A. Obergfell, B. A. Judd, M. A. del Pozo, M. A. Schwartz, G. A. Koretzky, and S. J. Shattil The Molecular Adapter SLP-76 Relays Signals from Platelet Integrin alpha IIbbeta 3 to the Actin Cytoskeleton J. Biol. Chem., February 16, 2001; 276(8): 5916 - 5923. [Abstract] [Full Text] [PDF]
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R. Goitsuka, A. Tatsuno, M. Ishiai, T. Kurosaki, and D. Kitamura MIST Functions through Distinct Domains in Immunoreceptor Signaling in the Presence and Absence of LAT J. Biol. Chem., September 14, 2001; 276(38): 36043 - 36050. [Abstract] [Full Text] [PDF]
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K. Sauer, J. Liou, S. B. Singh, D. Yablonski, A. Weiss, and R. M. Perlmutter Hematopoietic Progenitor Kinase 1 Associates Physically and Functionally with the Adaptor Proteins B Cell Linker Protein and SLP-76 in Lymphocytes J. Biol. Chem., November 21, 2001; 276(48): 45207 - 45216. [Abstract] [Full Text] [PDF]
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L. Kumar, V. Pivniouk, M. A. de la Fuente, D. Laouini, and R. S. Geha Differential role of SLP-76 domains in T cell development and function PNAS, January 22, 2002; 99(2): 884 - 889. [Abstract] [Full Text] [PDF]
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