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Blood, 1 March 2001, Vol. 97, No. 5, pp. 1352-1359
IMMUNOBIOLOGY
SH2 domain-mediated targeting, but not localization, of Syk in
the plasma membrane is critical for Fc RI signaling
Kiyonao Sada,
Juan Zhang, and
Reuben P. Siraganian
From the Receptors and Signal Transduction Section,
Oral Infection and Immunity Branch, National Institutes of Dental and
Craniofacial Research, National Institutes of Health, Bethesda, MD
Aggregation of the high-affinity IgE receptor induces the tyrosine
phosphorylation of subunits of the receptor and the subsequent association with the receptor of the cytosolic protein tyrosine kinase
Syk. The current experiments examined the functional importance of
membrane association of Syk and the role of the SH2 domain in
receptor-mediated signal transduction. Wild-type Syk and chimeric Syk
molecules with the c-Src myristylation sequence at the amino-terminus were expressed in a Syk-negative mast cell line. Chimeric Syk with the
myristylation sequence was membrane associated, and a small fraction
was constitutively colocalized with Fc RI, Lyn, and LAT
(linker for T-cell activation) in the glycolipid-enriched microdomains
or rafts. However, even under these conditions, the tyrosine
phosphorylation of Syk and the downstream propagation of signals
required FcRI aggregation. This chimeric Syk was less active than
wild-type Syk in FcRI-mediated signal transduction. In contrast, a
truncated membrane-associated form of Syk that lacked the SH2 domains
was not tyrosine phosphorylated by receptor aggregation and failed to
transduce intracellular signals. These findings suggest that SH2
domain-mediated membrane translocation of Syk is essential for
the FcRI-mediated activation of Syk for downstream signaling events
leading to histamine release. Furthermore, the localization of Syk in
glycolipid-enriched microdomains by itself is not enough to generate or
enhance signaling events.
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