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J. Biol. Chem., Vol. 277, Issue 42, 39401-39408, October 18, 2002
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From the Division of Vascular Biology, Department of Cell Biology,
The Scripps Research Institute, La Jolla, California 92037
Syk and ZAP-70 form a subfamily of nonreceptor
tyrosine kinases that contain tandem SH2 domains at their N termini.
Engagement of these SH2 domains by tyrosine-phosphorylated
immunoreceptor tyrosine-based activation motifs leads to kinase
activation and downstream signaling. These kinases are also regulated
by
The N-terminal SH2 Domains of Syk and ZAP-70 Mediate
Phosphotyrosine-independent Binding to Integrin
Cytoplasmic
Domains*
,
3 integrin-dependent cell
adhesion via a phosphorylation-independent interaction with the
3 integrin cytoplasmic domain. Here, we report that the
interaction of integrins with Syk and ZAP-70 depends on the N-terminal
SH2 domain and the interdomain A region of the kinase. The N-terminal SH2 domain alone is sufficient for weak binding, and this interaction is independent of tyrosine phosphorylation of the integrin tail. Indeed, phosphorylation of tyrosines within the two conserved NXXY motifs in the integrin 3 cytoplasmic
domain blocks Syk binding. The tandem SH2 domains of these kinases bind
to multiple integrin cytoplasmic domains with varying affinities
(3 (Kd = 24 nM) > 2 (Kd = 38 nM) > 1 (Kd = 71 nM)) as
judged by both affinity chromatography and surface plasmon resonance.
Thus, the binding of Syk and ZAP-70 to integrin cytoplasmic domains
represents a novel phosphotyrosine-independent interaction mediated by
their N-terminal SH2 domains.
*
This work was supported by National Institutes of Health
Grants HL 48728, HL 59007, and HL 31950.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of a post-doctoral fellowship from the Arthritis Foundation.
§
To whom correspondence should be addressed: Div. of Vascular
Biology, Dept. of Cell Biology, Scripps Research Inst., 10550 N. Torrey
Pines Rd., La Jolla, CA 92037. Tel.: 858-784-7124; Fax: 858-784-7343; E-mail: ginsberg@scripps.edu.
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