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(Received for publication, June 20, 1996, and in revised form, August 15, 1996)
From the The cytoplasmic tails of both the
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27962-27968
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
Laboratory of Immunology,
and 
subunits of the high affinity IgE receptor (Fc
RI) contain a
consensus sequence termed the immunoreceptor tyrosine-based activation
motif (ITAM). This motif plays a critical role in receptor-mediated
signal transduction. Synthetic peptides based on the ITAM sequences of
the and subunits of FcRI were used to investigate which
proteins associate with these motifs. Tyrosine-phosphorylated and
ITAM peptides immobilized on beads precipitated Syk, Lyn, Shc,
Grb2, and phospholipase C-1 from lysates of rat basophilic leukemia
RBL-2H3 cells. Syk was precipitated predominantly by the
tyrosine-diphosphorylated ITAM peptide, but much less by the
diphosphorylated ITAM peptide or by the monophosphorylated
peptides. Phospholipase C-1, Shc, and Grb2 were precipitated only by
the diphosphorylated ITAM peptide. Non-phosphorylated ITAM peptides
did not precipitate these proteins. In membrane binding assays, fusion
proteins containing the Src homology 2 domains of phospholipase C-1,
Shc, Syk, and Lyn directly bound the tyrosine-phosphorylated ITAM
peptides. Although the ITAM sequences of the and subunits of
FcRI are similar, once they are tyrosine-phosphorylated they
preferentially bind different downstream signaling molecules. Tyrosine
phosphorylation of the ITAM of the subunit recruits and activates
Syk, whereas the subunit may be important for the Ras signaling
pathway.
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