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CUTTING EDGE |
*
Department of Immunology, Medical Research Institute, Tokyo Medical and Dental University, Bunkyo-ku, Tokyo, Japan;
Department of Molecular Immunology, Biology III, Freiburg University, Freiburg, Germany; and
Tokyo Metropolitan Institute for Neuroscience, Fuchu, Tokyo, Japan
Activation signals of lymphocytes are negatively regulated by the membrane molecules carrying the immunoreceptor tyrosine-based inhibition motif (ITIM). Upon tyrosine phosphorylation, ITIMs recruit SH2-containing phosphatases such as SHP-1, resulting in down-modulation of cell activation. We showed that the cytoplasmic domain of the CD72 molecule carries an ITIM and is associated in vitro with SHP-1 upon tyrosine phosphorylation. Moreover, cross-linking of B cell Ag receptor (BCR) enhances both tyrosine phosphorylation of CD72 and association of CD72 with SHP-1 in B cell line WEHI-231. These results indicate that CD72 recruits SHP-1 upon tyrosine phosphorylation induced by BCR signaling, suggesting that CD72 is a negative regulator of BCR signaling.
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R. Lesourne, P. Bruhns, W. H. Fridman, and M. Daeron Insufficient Phosphorylation Prevents Fcgamma RIIB from Recruiting the SH2 Domain-containing Protein-tyrosine Phosphatase SHP-1 J. Biol. Chem., February 23, 2001; 276(9): 6327 - 6336. [Abstract] [Full Text] [PDF]
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