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J Biol Chem, Vol. 273, Issue 43, 28332-28340, October 23, 1998
From the Division of Human Immunology, Hanson Centre for Cancer
Research, Institute of Medical and Veterinary Science,
Adelaide, South Australia, 5000 Australia
Stimulation of platelet aggregation leads to
tyrosine phosphorylation of a number of receptors and signaling
molecules including platelet endothelial cell adhesion molecule-1
(PECAM-1). In this report, we demonstrate that both protein-tyrosine
phosphatases SHP-1 and SHP-2 physically associate with different
kinetics of assembly with tyrosine-phosphorylated human PECAM-1 during
integrin
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
IIb
3-mediated platelet
aggregation. Peptido-precipitation analysis revealed that
tyrosine-phosphorylated peptides encompassing residues 658-668 and
681-691 of PECAM-1 bound specifically to both protein-tyrosine phosphatases SHP-1 and SHP-2. We further show that the association of
SHP-1 with PECAM-1 occurs through the direct interaction of the
src homology region 2 domains of SHP-1 with two highly
conserved phosphotyrosine binding motifs within PECAM-1 having the
sequences NSDVQpY663TEVQV and DTETVpY686SEVRK
(where pY represents phosphotyrosine). In vitro
dephosphorylation experiments using phosphotyrosyl PECAM-1 peptides
encompassing either Tyr-663 or Tyr-686 revealed induction of SHP-1
catalytic activity, suggesting that PECAM-1 serves as a SHP-1
substrate. Surface plasmon resonance studies reveal that recombinant
SHP-2 binds PECAM-1 phosphopeptides with 5-fold higher affinity than recombinant SHP-1. These data suggest that in hematopoietic cells such
as platelets, PECAM-1 cellular signaling is regulated by the selective
recruitment and activation of two distinct protein-tyrosine phosphatases, SHP-1 and SHP-2, via a common immunoreceptor
tyrosine-based inhibitory-like motif.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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