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J Biol Chem, Vol. 274, Issue 17, 11505-11512, April 23, 1999
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From the The myeloid restricted membrane glycoprotein,
CD33, is a member of the recently characterized "sialic acid-binding
immunoglobulin-related lectin" family. Although CD33 can mediate
sialic acid-dependent cell interactions as a recombinant
protein, its function in myeloid cells has yet to be determined.
Since CD33 contains two potential immunoreceptor
tyrosine-based inhibition motifs in its cytoplasmic tail, we
investigated whether it might act as a signaling receptor in myeloid
cells. Tyrosine phosphorylation of CD33 in myeloid cell lines was
stimulated by cell surface cross-linking or by pervanadate, and
inhibited by PP2, a specific inhibitor of Src family tyrosine kinases.
Phosphorylated CD33 recruited both the protein-tyrosine phosphatases,
SHP-1 and SHP-2. CD33 was dephosphorylated in vitro by the
co-immunoprecipitated tyrosine phosphatases, suggesting that it might
also be an in vivo substrate. The first CD33
phosphotyrosine motif is dominant in CD33-SHP-1/SHP-2 interactions,
since mutating tyrosine 340 in a CD33-cytoplasmic tail fusion protein
significantly reduced binding to SHP-1 and SHP-2 in THP-1 lysates,
while mutation of tyrosine 358 had no effect. Furthermore, the
NH2-terminal Src homology 2 domain of SHP-1 and SHP-2,
believed to be essential for phosphatase activation, selectively bound
a CD33 phosphopeptide containing tyrosine 340 but not one containing
tyrosine 358. Finally, mutation of tyrosine 340 increased red blood
cell binding by CD33 expressed in COS cells. Hence, CD33 signaling
through selective recruitment of SHP-1/SHP-2 may modulate its ligand(s)
binding activity.
Cell Adhesion Laboratory,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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