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(Received for publication, February 4, 1997)
From the SHP-1 is a protein-tyrosine phosphatase
associated with inhibition of activation pathways in hematopoietic
cells. The catalytic activity of SHP-1 is regulated by its two SH2
(Src homology 2) domains;
phosphotyrosine peptides that bind to the SH2 domains activate SHP-1.
The consensus sequence (I/V)XYXX(L/V) is
present in the cytoplasmic tails of several lymphocyte receptors that interact with the second SH2 domain of SHP-1. In several of these receptors, there are two or three occurrences of the motif. Here we
show that the conserved hydrophobic amino acid preceding the phosphotyrosine is critical for binding to and activation of SHP-1 by
peptides corresponding to sequences from killer cell inhibitory receptors. The interaction of most SH2 domains with phosphopeptides requires only the phosphotyrosine and the three residues downstream of
the tyrosine. In contrast, the shortest peptide able to bind or
activate SHP-1 also included the two residues upstream of the phosphotyrosine. A biphosphopeptide corresponding to the cytoplasmic tail of a killer cell inhibitory receptor with the potential to interact simultaneously with both SH2 domains of SHP-1 was the most
potent activator of SHP-1. The hydrophobic residue upstream of the
tyrosine was also critical in the context of the biphosphopeptide. The
contribution of a hydrophobic amino acid two residues upstream of the
tyrosine in the SHP-1-binding motif may be an important feature that
distinguishes inhibitory receptors from those that provide activation
signals.
Volume 272, Number 20,
Issue of May 16, 1997
pp. 13066-13072
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
2 for the SH2 Domain-mediated Activation of the Tyrosine
Phosphatase SHP-1
,
Laboratory of Immunogenetics, NIAID,
National Institutes of Health, Rockville, Maryland 20852 and the
¶ Department of Cancer Biology, Cleveland Clinic Foundation
Research Institute, Cleveland, Ohio 44195
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